ANALYTICAL
BIOCHEMISTRY
r),
470-501
(1977)
A Compilation of Amino Acid Analyses of Proteins Xl. Residues
per Thousand
Residues,
3
DONALD M. KIRSCHENBAUM" department of Bioc~emisf~, Downstate Medical Center-SUNY, Brooklyn, New York 11203 Received October 29, 1976; accepted January 6, 1977
This paper, the third in a series (l), is a compilation of amino acid analyses of 312 proteins or proteinaceous materials which are listed in Table 1 by name and with their respective sources. In Table 2, the compositions data are reported as residues of amino acid per 1000 residues. The data were given in the references cited in various ways, e.g., percentage of moles of amino acid recovered, moles per 100 moles of amino acids, and percentage of residues. All such values have been changed to residues per 1000 residues, so that comparisons of the compositional data may be made. In addition to the amino acid analyses, the footnotes contain analytical values for carbohydrate, e.g., glucose, glucosamine, galactose, galactosamine, and sialic acid, and for amino acids not listed in Table 2 e.g., hydroxylysine and hydroxyproline. All analytical data reported were determined by column chromatography except for some tyrosine, tryptophan, and occasional half-cystine values. ACKNOWLEDGMENTS The Library of The Downstate Medical Center College of Medicine has been the major source of all publications examined. What was not avaiiable in the library was obtained for me from other libraries. I should like to thank the librarians for their most useful and #ntinuing assistance. During the summer of 1971- 1975, I was a Library Reader at the Library of the Marine Biological Laboratory, Woods Hole, Mass. I should like to thank the librarians of that library for their assistance. I thank Mr. E. Becker and Mr. D. Siegel for editing assistance. I thank Miss M. Colindreler, Mrs. F. Kuller, and Mrs. E. Levine for typing assistance.
REFERENCE 1. Kirschenbaum,
FOR TEXT
D. (1973) Anal. Biochem. 53,223; 56,208.
REFERENCES
FOR TABLE 2
1. Johnson, A. W., Wilhelm, .I. A., Ward, D. N., Hnilica, L. S. (1973) Biochim. Acta 295, 140. 2. Kobayashi, K. (1971) Immunochemistry 8,785. * Faculty Exchange Scholar, State University
Biophys.
of New York.
470 Copyright 0 1977 by Academic Press. Inc. AR rights of reproduction in any form reserved.
ISSN WQ3-2697
AMINO
ACID ANALYSES
OF PROTEINS
XI
471
3. Schrohenloher, R. E., Mestecky, J., and Stanton, T.-H. (1973) Biochim. Biophys. Actu 295, 576. 4. McIntosh, R. M., Kulvinskas, C., and Kaufman, D. B. (1971)Inr. Arch. Allergy 41,700. 5. Saha, A., Sambury, S., Smart, K., Heiner, D. C.. Sargent, A., and Rose, B. (1%9) J. Immunol. 102,476. -6. Schwick, H. G., Heimburger, N., and Haupt, H. (1966) 2. Inr. Med. 21, 193. 7. Heimburger, N., Haupt, H., and Schwick, H. G. (1971) in Proceedings of the International Research Conference on Proteinase Inhibitors (Fritz, H., and Tschesche, H., eds.), p. 1, W. deGruyter, Berlin. 8. Hamberg, U., Stelwagen, P., and Et-vast, H. S. (1973) Eur. J. Biochem. 40,439. 9. Hochstrasser, K., Reichert, R., Schwan, S., and Werle, E. (1974) Hoppe-Seyler’s 2. Physiol. Chem. 354,923. 10. Hochstrasser, K., Feuth, H., and Steiner, 0. (1974) Hoppe-Seyler’s Z. Physiol. Chem. 354, 927. 11. Crewther, W. G., Dobb, M. G., Dowling, L. M., and Hat-rap, B. S. (1968) in Symposium on Fibrous Proteins (Crewther, W. G., ed.), p. 329, Butterworths, Reading, Mass. 12. Cotfield, M. C., Fletcher, J. C., and Robson, A. (1968) in Symposium on Fibrous Proteins (Crewther, W. G., ed.), p. 299, Butterworths, Reading, Mass. 13. Hermier, J., Lebeault, J. M., and Zevaco, C. (1970) Bull. Sot. Chim. Biol. 52, 1089. 14. Nagaoka, K., and Yamada, Y. (1974) Agr. Biol. Chem. 37, 2791. 15. Simons, K., Ehnholm, C., Renkonen, O., and Bloth, B. (1970) Acta Path. Microbial. Stand. 78B, 459. 16. Fidge, N. (1973) Biochim. Biophys. Acta 295, 258. 17. Shore, V. G., and Shore, B. (1973) Biochemistry 12, 502. 18. Havel, R. J., and Kane, J. P. (1973) Proc. Nat. Acad. Sci. USA 70, 2015. 19. Shore, V. G., Shore, B., and Hart, R. G. (1973) Biochemistry 13, 1579. 20. Ayrault-Jarrier, M., Lastra, G., Pastier, D., Burdin, J., and Polonovski, J. (1972) Biochimie 54, 973. 21. Blaton. V., Peeters, H., Vercaemst, R., Vandecasteele, N., and Caster, H. (1974) Biochemistry 13, 1127. 22. Kostner, G. (1972) Biochem. J. 130, 913. 23. Swann, D. A., and Radin, E. L. (1972) J. Biol. Chem. 247, 8069. 24. Stimson, W. H., and Scott, L. E. (1972) FEBS Letf. 23, 298. 25. Cassman, M., and Vetterlein, D. (1974) Biochemistry 13, 684. 26. Siegel, L., and Englard, S. (1962) Biochim. Biophys. Acru 64, 101. 27. Marshall, C. L., Wicken, A. J., and Brown, A. D. (1969) Canad. J. Biochem. 47, 71. 28. Stoeckenius, W., and Kunau, W. H. (1%8) J. Cell Biol. 38, 337. 29. (a) Bakerman, S., and Wasemiller, G. (1%7)Biochemistry 6, 1100; (b) Tanner, M. J. A., and Gray, W. R. (1971) Biochem. J. 125, 1109; (c) Chapman, D. (1972) in Polymerization in Biological Systems, Ciba Foundation Symposium No. 7, p. 261, Elsevier, Amsterdam; (d) Palmer, F. B. St. C., and Verpoorte, J. A. (1971) Canad. J. Biochem. 49, 337. 30. Hamaguchi, H., and Cleve, H. (1971) Biochim. Biophys. Acra 233, 320. 31. Passow, H. (1969) Progr. Biophys. Mol. Biol. 19, 425. 32. (a) Zwaal,R. F. A., andVanDeenen, L. L. M. (1968)Biochim. Biophys. Acra 150,323; (b) Rosenberg, S. A., and Guidotti, G. (1%9) J. Biol. Chem. 244, 5118. 33. Mazia, D., and Ruby, A. (1968) Proc. Nat. Acad. Sci. USA 61, 1005. 34. (a) Pellett, P. L., Pascoe. E., and Shaafi, R. I. (1972) Comp. Biochem. Physiol. 41B, 483; (b) Kobylka, D., and Carrway, K. L. (1972b) Biochim. Biophys. Actu 288, 282. 35. Mattel, M. B., Dubois, P., and Got, R. (1973) Biochim. Biophys. Acru 311, 565. 36. Chien, H. C., and Richardson, T. (1967) J. Dairy Sci. 50, 1868. 37. Brunner, J. R. (1967) in Structural and Functional Aspects of Lipoproteins in Living Systems (Tria, E., and Scanu, A. M., eds.), p. 545, Academic Press, New York.
472
DONALD
M. KIRSCHENBAUM
38. Spenny, J. G., Saccomani, G., Spitzer, H. L., Tomana, M., and Sachs, G. (1974)Arch. Biochem. Biophys. 161,456. 39. Mahieu, P. M., and Winand, R. J. (1973) Eur. J. Biochem. 37, 157. 40. Mahieu, P. M., and Winand, R. J. (1970) Eur. J. Biochem. 12,410. 41. Marquardt, H., Wilson, C. B., and Dixon, F. J. (1973) Biochemistry 12, 3260, 42. Westberg, N. G., and Michael, A. F. (1970) Biochemistry 9, 3837. 43. Beisswenger, P. J., and Spiro, R:G. (1970) Science 168, 5%. 44. (a) Kefalides, N. A. (1970a) in Chemistry and Molecular Biology of Interce~ular Matrix (Balazs, E. A., ed.), Vol. 1, p. 535, Academic Press, New York; (b) Funs, K. K., and Kalant, N. (1972) Biochem. J. 129, 733. 45. Kefalides, N. A. (1%8) Biochemistry 7, 3103. 46. Hudson, B. G., and Spiro, R. G. (1972) J. Biol. Chem. 247,4229. 47. Bomens, M., and Kasper, C. B. (1973) J. Bid. Chem. 248, 571. 48. Barber, A. J., and Jamieson, G. A. (1970) J. Biol. Chem. U&6356. 49. Meldolesi, J., and Cova, D. (1972) J. Cell Eiol. SJ, 1. 50. Hjerten, S., and Johansson, K. E. (1972) Biochim. B~ophys. Acta 288,3 12. 5 1. Weser, U., Rupp, H., Donay, F., Linnemann, F.. Voelter, W., Voetsch, W., and Jung, G. (1973) Eur. J. Biochem. 39, 127. 52. Winge, D. R., and Rajagopalan, K. V. (1972)Arch. Biochem. Biophys. 153, 755. 53. Kagi, J. H. R. (1970) Eighth-International Congress of Biochemistry, Switzerland Abstracts, p. 130. 54. Surguchev, A. P., Surgucheva, I. G., Ermorhina, T. M., and Zaitseva, G. N. (1971) *Eiokhimiyh 36, 791. 55. Tokuyama, H. ‘(1973) Blochim. Biophys. Actu 317, 338. 56. Hunt, S., and Jevons, F. R. (1965) B~ochem. J. 97,701. 57. DeSalegui, M., and Plonska, H. (1%9) Arch. Biochem. Biophys. 129, 49. 58. Rossi, E., and Stall, E. (1968) in Biochemistry of Glycoproteins and Related Substances, Part 2, pp. 72-73, S. Karger, Basel. 59. Lombart, C., and Winzler, R. J. (1972) Biochem. J. 128, 975. 60. Huser, H., Mody, E., and Faillard, H. (1973)Hoppe-Seyler’sZ. Physiol. Chem. 354,749. 61. Neiderhiser, D. H., Plantner, J. J., and Carlson, D. M. (1971)Arch. Biochem. Biophys. 145, 155. 62. Degand, P., Roussel, P., Lamblin, G., and Havez, R. (1973) Biochim. Biophys. Acta 320, 318. 63. Lamblin, G., Lhermitte, M., Degand, P., Sergeant, Y. H., and Roussel, P. (1973) Biochim. Biophys. Acta 322,372. 64. Tung, K. K., Rosenthal, A., and Nordin, J. H. (1971) J. Biol. Chem. 246,6722. 65. Wolfram, F., and Kotorii, K. (1968) J. Neurochem. l&1281; see also Eng, L. F., Chao, F. C., Gerstl, B., Pratt, D., and Tavastsjema, M. G. (1968) Biochemistry 7, 4455. 66. Wolfram, F., and Tourtellotte, W. W. (1972) Neurology 22, 1044. 67. (a) Hegstrand, L. R., and Komguth, S. E. (1973) Biochim. Biophys. Acta 317, 380; (b) Deibler, G. E., Martenson, R. E., and Kies, M. W. (1972) Prep. Biochem. 2, 139. 68. Puett, D., Friebele, E., and Hammonds, Jr., R. G. (1973) Biochim. Biophys. Acru 328, 261. 69. Hayashi, Y. (1972) J. Biochem. (Tokyo) 72,83. 70. Mani, R. S., and Kay, C. M. (1973) Canad. J. Biochem. 51, 178. 71. Bodwell, C. E., Hepner, P. A., Brooks, B., and Hagan, S. (1971)Int. J. Biochem. 2,682. 72. LeStourgeon, W. M., and Rusch, H. P. (1973) Arch. Biochem. Biophys. 155, 144. 73. (a) Olson, M. 0. J., Orrick, L. R., Jones, C., and Busch, H. (1974) J. Biol. Chem. 249, 2823; (b) Grogan, D. E., Desjardins, R., and Busch, H. (1%6) Cancer Res. 26,775; (c) Teng, C. S., Teng, C. T., and Allfrey, J. G. (1971) J. Biol. Chem. 2.46, 3597. 74. Neu, H. C. (1%7) J. Biol. Chem. 242,38%.
AMINO
ACID ANALYSES
OF PROTEINS
XI
473
75. Degens, C. T., Spencer, D. W., and Parker, R. H. (1967) Comp. Biochem. Physiol. 20, 553. 76. Meenakshi, V. R., Hare, P., and Wilbur, K. M. (1971) Comp. Biochem. Physiol. 40B, 1037. 77. Degens, E. T., and Love, S. (1965) Nature (London) 205,876. 78, Carmichael, D. .I., Dodd, C. M., and Nawrot, C. F. (1974) C&if. Tissue Res. 14, 177. 79. Sleigh, R. W., Melrose, G. J. H., and Smith, M. B. (1973)~~~~h~rn. Biophys. Acfu 310, 453. 80. Skinner, M., and Cohen, A. S. (1973) Biochem. Biophys. Res. Commun. 54, 732. 81. Anstee, D. J., and Pardoe, G. I. (1973) Eur. J. Biochem. 39, 149. 82. Halsey, J. F., and Harrington, W. F. (1973)Biochemistry 12, 693. 83. Havir, E. A., and Hanson, K. R. (1973) Biochemistry 12, 1583. 84. Beuving, G., and Gmber, M. (1971) Biochim. Biophys. Acta 232, 524. 85. Yamamoto, S., Minoda, Y., and Yamada, K. (1972) Agr. Biol. Chem. 36, 2097. 86. Yurewicz, E. C., Ghalambor, M. A., Duckworth, D. H., and Heath. E. C. (1971)5. B&Z. Chem. 246,X07. 87. Baden, H. P., Goldsmi~, L. A., and Fleming, B. (1973)Biockim. ~~~phys. Actu 317,303. 88. Berg, R. A., and Prockop, D. J. (1973) Biochemistry 12, 3395. 89. Thompson, H. C., and Thompson, M. H. (1970) Comp. Biochem. Physiol. 35,471. 90. Yui. C. (1971) J. Biochem. (Tokyo) 69, 101. 91. Ohkawa, I., Kageyama, M., and Egami, F. (1973) J. Biochem. (Tokyo) 73, 281. 92. Tono, H., and Komberg, A. (1967) .I. Biol. Chrm. 242, 2375.
474
DONALD
M. KIRSCHENBAUM TABLE PROTEIN
Number 1 Name Source
2 Name Source 3
Name Source
4 Name Source 5
6
Name .Source Name Source
7 Name Source
8 Name Source
9 Name Source 10
11
Name Source Name
12
Source Name
13
Source Name
14
Source Name
15
Source Name Source
16 Name Source
1 INDEX
Number Histone, fraction 1 Sea urchin (Strongylo-
17 Name
centrotus pluteus)
18
putpuratus
nuclei Histone, fraction 2 Sea urchin (S. purpuratus pluteus) nuclei Histone, fraction 3 Sea urchin (S. purpuratus pluteus) nuclei Histone, fraction 4 Sea urchin (S. purpuratus pluteus) nuclei Histone, fraction 5 Sea urchin (S. purpuratus pluteus) nuclei Histone, fraction 6 Sea urchin (S. purpuratus pluteus) nuclei Immunoglobulin, secretory piece, bound Human colostrum Immunoglobulin, J chain Human myeloma IgA protein Fe1 Immunoglobulin, IgG Human supemate serum after cryoprecipitation Immunoglobulin, IgG Human, pooled Inhibitor, proteinase: a,-anti-trypsin Human serum Inhibitor, proteinase: o-anti-chymotrypsin Human serum Inhibitor, proteinase: IIntero-trypsin inhibitor Human serum Inhibitor, proteinase: anti-thrombin Human serum Inhibitor, proteinase: Cl-inactivator Human sentm Inhibitor, proteinase: cy,-macroglobulin Human serum
19
Source Name Source Name Source
20 Name Source
21 Name Source
22 Name Source
23 Name Source
24 Name Source
25 Name Source
26 Name Source
27 Name Source
28 Name Source
29 Name Source
30 Name Source
31 Name Source
32 Name Source
Source
34 Name Source
Inhibitor, proteinase Human bronchial mucus Inhibitor, proteinase Human plasma Kerateine, S-carboxymethyl-, (SCMK-A) a-Keratin of Merino wool y-Keratose Oxidized wool Leucine dehydrogenase Bacillus
subtilis
Lipase, F-3A Mucor
lipolyticus
Lipase, F-3B Mucor
lipolyticus
Lipoprotein, Lp (a) Human plasma Lipoprotein, very low density Pig plasma Lipoprotein, very low density, Band B Human plasma Lipoprotein, very low density, Band C Human plasma Lipoprotein, very low density, Band D Human plasma Lipoprotein, very low density, Band E Human plasma Lipoprotein, very low density, Band F Human plasma Lipoprotein, very low density, Band H Human plasma Lipoprotein, very low density, arginine-rich Human (with dysbetalipoproteinemia) Lipoprotein, very low density, arginine-rich Human (hyperlipemic) Lipoprotein, very low density Rabbit serum
AMINO
ACID ANALYSES TABLE
Source
36 Name 31
Source Name Source
38 Name Source
39 Name 40 41 42
Source Name Source Name Source Name Source
43 Name
44
Source Name Source
45 Name Source
46 Name Source
47 Name Source
48 Name 49
50
51 52 53
Source Name Source Name Source Name Source Name Source Name Source
475
XI
1 (Continued) Number
Number 35 Name
OF PROTEINS
Lipoprotein, very low density Rabbit serum, cholesteremic Lipoprotein, low density U-J%) Rabbit serum Lipoprotein, low density U-DU Rabbit serum, cholesteremic Lipoprotein, low density U-DL,) Rabbit serum, cholesteremic Lipoprotein, low density (U) Pig plasma Lipoprotein, low density(D) Pig plasma Lipoprotein, low density Human plasma Lipoprotein 2, high density W) Pig plasma Lipoprotein 2, high density UN Pig plasma Lipoprotein 3, high density WI Pig plasma Lipoprotein, apo-high density, CYP Human serum Lipoprotein, soluble, aP, Lipoprotein #45 Lipoprotein, gellable, CUP, Lipoprotein #45 Lipoprotein, apo-high density (HDL,) Chimpanzee plasma Lipoprotein, apo-high density (HDL,) Chimpanzee plasma Lipoprotein B Human serum HDL, Lubrication factor Bovine synovial fluid a-Macroglobulin Human (female) serum Malic dehydrogenase, form a Bovine heart, cytoplasmic
54 Name Source
55 Name Source
56 Name Source
57 Name Source
58 Name Source
59 Name Source
60a Name 60b
Source Name Source
6Oc Name Source 61 Name Source
62 Name Source
63 Name 64
65 65a 66
Source Name Source’ Name Source Name Source Name Source
66a Name Source
67 Name Source
88a Name Source 68b Name Source
69 Name Source
Malic dehydrogenase, form b Bovine heart, cytoplasmic Malic dehydrogenase Bovine heart, mitochondria Malic dehydrogenase Bovine heart, supemate Membrane protein, defatted Halobacterium
halobium
cell envelope Membrane, purple H. halobium
Membrane, gas vacuole, (inttacytoplasmic) H. halobium
Membrane protein Human erythrocyte Membrane Human erythrocyte Membrane Human erythrocyte Membrane, water soluble protein Human erythrocyte Membrane protein Human erythrocyte Membrane protein Human erythrocyte Membrane Human erythrocyte Membrane Human erythrocytes Membrane Bovine erythrocytes Membrane Cat (Felis domesticus) erythrocyte Membranes, fat globules Bovine milk Membrane, fat globules Human milk Membranes, peak I Canine gastric cell Membranes, peak II Canine gastric cell Membranes, glomexular basement Human kidneys
476
DONALD
M. KIRSCHENBAUM
TABLE Number Membranes, glomerular basement Source Human kidneys 71 Name Membranes, tubular basement Source Human kidneys 72 Name Membranes, glometular basement Source Human kidneys 73 Name Membranes, glometular basement Source Human kidneys 74 Name Membranes, glomerular basement Source Human kidneys, diabetes mellitus 75 Name Membranes, glomerular basement Source Human kidneys 76 Name Memb~nes, gIome~lar basement Source Canine kidneys 77 Name Membranes, glomerular basement Source Ovine kidneys 78 Name Membranes, glometular basement Source Rat kidneys 78a Name Membranes, glometular basement Source Rat kidney 78b Name Membranes, glomerular basement Source Rat kidney, antiserum nephrosis 79 Name Membranes, glomerular basement Source Bovine kidneys 80 Name Membranes, nuclear Source Rat liver 81 Name Membranes Source Human platelets 82a Name Membranes, zymogen granule Source Guinea pig pancreas 82b Name Membranes, rough microsomes Source Guinea pig pancreas 82~ Name Membranes, smooth mierosomes
1 (Co~finued) Number
70 Name
83 84 85 86 87 88
88a 89
Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source
Guinea pig pancreas Membranes Acholeplasma
Me~~o~ionein Rat liver Metallothionein Rat liver Met~lo~ionein Chicken liver Metallothionein Horse liver Methionyl-RNA BuciEius
laidlawii
synthetase
brevis
Microsomes Rabbit muscle Mitogen, fraction E-2 Shoriku (Phytolacca esculenta)
90 91
Name Source Name Source
92 93 94 95 96
Name Source Name Source Name Source Name Source Name Source
97 98 99
Name Source Name Source Name Source
100
101 102
Name Source Name Source Name Source
103 Name 104
Source Name Source
Mitogen, fmction E-3 Shoriku (P. esculenta) Mucin Whelk (Buccinum undatum) hypobranchial Mucin, major Porcine submaxillary gland Mucin, minor Porcine submaxillary gland Mucin Porcine submaxillary gland Mucin Canine submaxillary gland Mucin Canine submaxillary gland Mucin, major Bovine submaxillary gland Mucin, minor Bovine submaxillary gland Mucin, major Ovine submaxillary gland Mucin, minor Ovine submaxillary gland Mucin, Gottschalk Ovine submaxillary gland Mucin Bovine sublingual gland Mucin Equine submaxillary gland Mucin A Porcine gall bladder
AMINO
ACID ANALYSES TABLE
Number 105
106 107 108 109
Name Source Name Source Name Source Name Source Name Source
110 Name 111
Source Name Source
112 Name 113 114 115 116 117 118
Source Name Source Name Source Name Source Name Source Name Source Name Source
119 Name 120
Source Name Source
121 Name Source
122 Name Source
123 Name Source
124 Name Source
124a Name 125
Source Name Source
OF PROTEINS
477
XI
1 (Continued) Number
Mucin H Porcine gall bladder Mucin (Fucomucine) Human bronchiogenic cyst Mucin (Sulfomucine) Human bronchiogenic cyst Mucin (Sialomucine) Human bronchiogenic cyst Mucin, neutral (from Sepharose) Human bronchial Mucin, neutral (from CMcellulose) Human bronchial Mucin, neutral (from CMcellulose) Human bronchial Mycodextranase, fast Penicillium
127 128 129 130 131 132 133
Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source
134 Name Source
135 Name
melinii
Mycodextranase,
126 Name
slow
P. melinii
Myelin Human centrum ovale Myelin Monkey centrum ovale Myelin Bovine centrum ovale Myelin Bovine optic nerve Myelin Bovine spinal cord white matter Myelin Human brain white matter Myelin Human brain MS white matter Myelin Human brain plaque edges Myelin Human brain plaque Myelin, basic protein Bovine, adult Myelin, basic protein Bovine, fetal Myelin, basic protein Bovine spinal cord Myoglobin I Turtle heart
Source
136 Name Source
137 Name Source
138 Name Source
139 Name Source
140 Name Source
141 Name Source
142a Name Source
142b Name Source
142~ Name Source
143 Name Source
144 Name
Myoblobin II Turtle heart Myoglobin III Turtle heart Myoglobin I Bovine heart Myoglobin II Bovine heart Myoglobin III Bovine heart Myoglobin IV Bovine heart Myosin, g-subunit Rabbit skeletal muscle Myosin, light chain (LC,) Rabbit cardiac muscle Myosin, light chain (LC,) Rabbit cardiac muscle Myosin Bovine muscle Myosin Porcine muscle Myosin Rabbit muscle Myosin Human uterus smooth muscle Myosin Human pectoral striated muscle Nuclei, phenol-soluble fraction Physarum
polycephalum
plasmodia Nucleoli, phenol-soluble fraction P. polycephalum plasmodia Nucleoli Rat Novikoff hepatoma ascites Nuclei, phenol-soluble protein fraction Rat liver Nuclei, phenol-soluble protein fraction Rat kidney 5’-Nucleotidase Escherichia
coli
Organic matrix
478
DONALD
M. KIRSCHENBAUM
TABLE Number Source
145 Name Source
146 Name Source
147 Name Source
148 Name Source
149 Name Source
150 Name Source
151 Name Source
152 Name Source
153 Name Source
154 Name Source
155 Name Source
156 Name Source
157 Name 158 159 168 161 162 163
Source Name Source Name Source Name Source Name Source Name Source Name Source
164 Name 165 166 167 168
Source Name Source Name Source Name Source Name
1 (Conrinued) Number
Argonauta
hians
egg
case
Organic matrix Loligo pen Organic matrix Nautilus
Source
170 Name
pompilius
Organic matrix Sepia cuttle bone Organic matrix Spirula spirula shell Organic shell matrix Achatinella
lorata
Organic shell matrix Acmaea
pustulata soluta willcoxi
Architectonica
nobilis
Organic shell matrix caelata
Organic shell matrix Bulla
Source
173 Name Source
174 Name 175 Name 176 Name Source
Organic shell matrix
Astraea
Source
172 Name
Source
Organic shell matrix Aplysia
Source
171 Name
Source
Organic shell matrix Akera
Janthina
169 Name
177 Name Source
178 Name Source
179 Name Source
striata
Organic shell matrix Cavolina
tridentata
Organic shell matrix Colus
trophius
Organic shell matrix Crepidula
fornicata
Organic shell matrix Crepidula
plana
Organic shell matrix Cypraea
scapula
Organic sheU matrix Epitonium
ongulatum
Organic shell matrix Fissurella
barbadensis
(from Puerto Rico) Organic shell matrix F. barbadensis (from Cuba) Organic shell matrix Gastropod (indefinable) Organic shell matrix Haliotis
crachfordi
Organic shell matrix Helisoma
Source
181 Name Source
182 Name Source
183 Name Source
zebra
Organic shell matrix Dolabella
180 Name
trivalvis
Organic shell matrix
184 Name Source
185 Name Source
186 Name Source
187 Name Source
188 Name Source
189 Name Source
190 Name Source
191 Name
janthina
Organic shell matrix Littorina
littorea
Organic shell matrix Lunatia
trisseriata
Organic shell matrix L. trisseriata operculum Organic shell matrix Melanella
martini
Organic shell matrix Murex
brevtfrons
Organic shell matrix Nerita
plexa
Organic shell matrix N. plexa operculum Organic shell matrix Nassarius
trivittatus
Organic shell matrix Oxynoe
viridis
Organic shell matrix Planorbis sp. Organic shell matrix Polinices
duplicatus
(Provincetown, Mass.) Organic shell matrix P. duplicatus (Texas) Organic shell matrix P. duplicatus (Texas) Organic shell matrix P. duplicatus (Florida) Organic shell matrix P. duplicatus (North Carolina) Organic shell matrix Siphonaria
alternata
Organic shell matrix Succinea
ovalis
Organic shell matrix Turitella
terebra
Organic shell matrix Umbraculum
indicum
(Indonesia) Organic shell matrix CJ. indicum (Hawaii) Organic shell matrix Urosalpinx
cinera
Organic shell matrix Viviparus
georgianus
Organic shell matrix
AMINO
ACID ANALYSES TABLE
Number Source
192 Name Source
193 Name Source
194 Name Source
195 Name 1%
Source Name Source
197 Name Source
198 Name 199 200 201
Source Name Source Name Source Name Source
202 Name Source
203 Name 204 205
Source Name Source Name Source
206 Name Source
207 Name 208 209
Source Name Source Name Source
210 Name
OF PROTEINS
479
XI
1 (C~~~j~~e~) Number
Aequipecten
irradians
(Woods Hole, Mass.) Organic shell matrix A. irradians (Woods Hole, Mass.) Organic shell matrix Anadara
transversa
(Woods Hole, Mass.) Organic shell matrix A. transversa (Mississippi Delta) Organic shell matrix A. transversa (Texas) Organic shell matrix A. transversa (Mississippi Delta) Organic shell matrix A. transversa (Campeche, Mexico) Organic shell matrix Arctica
Organic shell matrix consobrina
Organic shell matrix Crassostrea
virginica
Organic shell matrix Laevicardium
hyalina
Organic shell matrix Macoma tenta (Woods Hole, Mass.) Organic shell matrix M. tenta (Woods Hole, Mass.) Organic shell matrix Malletia sp. Organic shell matrix Mercenaria
212 Name Source
213 Name Source
214 Name Source
215 Name Source
216 Name Source
217 Name Source Source
219 Name Source
220 Name Source
221 Name Source
222 Name Source
compressus
Organic shell matrix Lyonsia
Source
mortoni
(Woods Hole, Mass.) Organic shell matrix L. mortoni (Woods Hole, Mass.) Organic shell matrix Limopsis
211 Name
218 Name
islandica
Corbicula
Source
mercenaria
Organic shell matrix Mulina laieralis (Salem, Mass.) Organic shell matrix
223 Name Source
224 Name Source
225 Name Source
226 Name Source
227 Name Source
228 Name Source
lateralis (Woods Hole, Mass.) Organic shell matrix M. lateralis (Woods Hole, Mass.) Organic shell matrix M. lateralis (Woods Hole, Mass.) Organic shell matrix M. lateralis (New York) Organic shell matrix M. lateralis (Long Island, N.Y.) Organic shell matrix M. lateralis (SapelloIsland, Ga.) Organic shell matrix M. lateralis (Louisiana) Organic shell matrix M. lateralis (Louisiana) Organic shell matrix M. lateralis (Texas) Organic shell matrix M. lateralis (Texas) Organic shell matrix M. lateralis (Compeche, Mex.) Organic shell matrix Mytilus edulis (Woods Hole, Mass.) Organic shell matrix M. edulis (Woods Hole, Mass.) Organic shell matrix M.
Neotrigonia
margaritacea
Organic shell platrix Nucula proxima (Woods Hole, Mass.) Organic shell matrix N. proxima (Woods Hole, Mass.) Organic shell matrix Nucula truncula (Woods Hole, Mass.) Organic shell matrix N. proxima (Woods Hole, Mass.) Organic shell matrix Per~ploma
leanum
DONALD
480
M. KIRSCHENBAUM
TABLE
Number
Number 229 230 231
Name Source Name Source Name Source
232
Name Source
233
Name Source Name Source Name Source
234 235
236
237
Name Source Name Source
238a Name 238b
pholad~ormis
Organic shell matrix Pitar cordata (Texas) Organic shell matrix Pitar morrhuana (Woods Hole, Mass.) Organic shell matrix P. morrhuana (Woods Hole, Mass.) Organic shell matrix Sax~domus
Source
L. irrorata
239b Name
Source
242b Name Source
243a Name Source
243b Name Source
244 Name
nuttali
Organic shell matrix Tagelus divisus (Bermuda) Organic shell matrix T. divisus (Long Island, N.Y.) Organic shell matrix Yoldia limatula (Woods Hole, Mass.) Organic shell matrix Y. limatula (Woods Hole, Mass.) Organic matrix protein, insoluble Littorina
Source
24Qa
Organic shell matrix Petricola
Source Name
239a Name
1 (Continued)
irrorata
Organic matrix protein, solubie
P. duplicatus
Source
Thais
247 Name Source
248 Name Source
249 Name Source
250 Name Source
251 Name 252 Name Source
duplicatus
Organic matrix protein, soluble
Source Name
246
Source
Organic matrix protein, insoluble Polinices
245
Source Name Source Name Source
Organic matrix protein, insoluble floridana
253 Name Source
254 Name Source
240b Name
Organic matrix protein, soluble
255 Name
Source 241a Name
T. floridana
P. virens
Source 256 Name Source 257 Name Source 258 Name Source
Organic matrix protein, insoluble
259 Name
Source
241b Name Source
242a Name
Organic matrix protein, insoluble Pila
virens
Organic matrix protein, soluble
~a~&~orna
de&sum
Organic matrix protein, soluble.. C. decisum
Organic matrix protein, insoluble Nassarius
obsoletus
Organic matrix protein, soluble Nassarius
Organic matrix (recent) shell Organic matrix Planorbis supremus shell Organic matrix Pianorbis
P. supremus-revertens
shell Organic matrix Planorbis
shell
revertens
Organic matrix Planorbis
shell
oxystoma
Organic matrix Pianorbis
troch~ormis
shell Organic matrix Planorbis
planorbiformis
shell Organic matrix Pianorb~s
sulcatus
shell
Organic matrix Planorbis heimensis
tenuis-stein-
Planorbis
steinheimensis
shell Organic matrix
shell Organic matrix protein, acid extracted Rat teeth Organic matrix protein, acid extracted Rat, Lathyritic, teeth Periostracum Mollusc (Akera soluta) Periostracum Moilusc (Aplysia willoxi) Periostracum Mollusc (Dollabella scapula)
Periostracum
AMINO
ACID ANALYSES TABLE
261
Source Name Source Name Source
1 (Continued)
Mollusc(Hydanrinaphysis)
Periostracum Mollusc (Arctica Periostracum Mollusc (Corbicula
273 islandica)
274 275
consobrina) 262 263
264a 264b 265
266a
Name Source Name Source Name Source Name Source Name Source Name Source
266b Name Source 266~
Name Source
267a Name Source
267b Name 268
Source Name Source
Periostracum Mollusc (Mulinia lateralis) Periostracum Mollusc (Mythilus edulis) Periostracum Mollusc (Pitar morrhuana) Periostracum Mollusc (P. morrhuana) Periostracum Mollusc (Solemya velum) Periostracum Mollusc (Tagelus divisus) Bermuda Periostracum Mollusc (T. divisus) Nantucket Island Periostracum Mollusc (T. divisus) Long Island, N.Y. Periostracum Mollusc (Yoldia limulara) Periostracum Mollusc ( Y. limulata) Periostracum Mollusc (Nautilus
Name Source Name Source Name Source
270 271 272
Name Source Name Source Name Source Name Source
Ovomucin (a) Chicken egg white Ovomucin (b) Chicken egg white Ovomucin I Chicken egg white Ovomucin D Chicken egg white
P Component Human spleen amyloid P, substance Sheep hydrated cyst fluid Paramyosin Clam (Mercenaria mercenaria)
276 277
278 279 280
281 282 283 284
Name Source Name Source Name Source Name Source Name
Paramyosin, light Clam (M. mercenaria) Phenylalanine-ammonia lyase Potato Phosvitin Rooster plasma Phytase Aspergillus
terreus
Polysaccharide erase
depolym-
Source Name Source Name Source Name Source Name Source
Aerobacter
aerogenes
Name Source Name Source
Pyocin R sheath
Prekeratin Cow snout Procollagen-C Chick tendon Protocollagen-C Chick tendon Protocollagen White shrimp (Penaeus setiferus)
285 286
pompilius) 269
481
XI
Number
Number
260
OF PROTEINS
287
Name Source
288
Name Source
Pseudomonas
aeruginosa
Pyocin S, Pseudomonas
aeruginosa,
strain M 47 lysate Pyrophosphatases, inorganic Bacillus subtilis, strain B 133, vegetative cell Pyrophosphatases, inorganic B. subtilis, strain B 133, spore
32 20
89
88 50
26
40
65 51
100
Leucine
lsoleucine
Protine
Serine
Threonine
308
21
tP
91
118
Methionine
Lysine
Amide
11111123
-----_
Tyrosine Tryptophan
Reference
5
20
-----_
Phenylalanine
ammonia
7
24
21
Arginine Histidine
7t13
10
acid
Glutamic Half-cystine
-1
9
acid
Aspartic
79
61
21 13
26
54
33 273
2
Valine
1”
114 121
acid
Alanine
Glycine
Amino
12
14
8
47
249
-1
83
54 34
48
67
47 27
48
61 207
3
4
29
22
29
90
97
tP
89
34 67
68
34
103 34
62
111 134
4
29
20
29
89
97
7
t13
78
36 61
58
38
106 36
59
115 134
5
37
17
27
80
139
16
-1
84
60 51
86
32
62 59
65
70 121
6
-3
22
43
32
9
49
57
0
27
107
56 107
74.
50
95 34
82
99 57
7
-
0
42.7
8.8
8.3
73.6
45.6
7.2
50.3
116.3
99.3 165.8
66.8
63.9
60.1 51.1
74.0
193 46.8
8
COMPOSITIONAL
4
-
-
36.5
32.6
20.2
31.7
67.8
5.4
5.8
102.9
81.7 81.2
138.4
739’
75.8 21.1
83.8
75.1 56.1
9
DATA:
45
-
37.5
34.6
11.9
30.7
57.3
7.2
2
102.1
87.0 83.5
124
75.74
84.5 23.6
87.8
73.4 57.2
10
Residues 111%
6
14.58
5.5
21.4
76.3
33.3
23.3
84.1
21.4
0
129.2
56.6 97.5
35.2
32.6
99.0 38.9
47.4
6
12.6’
8.0
23.6
55.8
18.0
34.9
53.0
22.8
0
102.7
46.5 79.7
39.7
22.0
90.5 33.8
36.5
13.4 32.8
12’59
6
14.48
16.9
40.1
50.0
22.0
51.8
56.3
20.0
16.9
119.7
46.4 95.0
48.7
36.9
74.0 39.1
58.6
29.0 33.7
13160
1000 residues
PER 1000 RESIDUES per
23.8 35.5
TABLE 2 RESIDUES
7
12.19
19.9
31.3
57.2
11.2
47.0
66.5
21.7
9.3
117.0
37.8 86.0
43.8
32.4
72.3 35.7
43.2
17.5 35.3
14161
7
24.9”’
13.1
26.4
41.4
15.9
27.2
44.3
17.9
5.5
76.4
58.8 59.2
43.4
35.3
70.9 22.6
35.9
9.3 24.9
1p2
7
12.3’r
13.0
47.5
46.3
28.5
38.6
57.5
16.3
15.2
122.9
53.6 70.8
55.1
39.6
77.7 31.6
69.3
27.5 35.0
16rG3
10
-13
-12 9
47 -
58
42 -
60
5
103
127
99
45
5.2
90
24
72
34
63 42
18
53 -
39
21
42
63
58
81
84
139
63
41
94
62 38
34
38
48
17
II
104
42 -14
28
6
74
34
5
71
141
80
94 47
40
% 33
63
88 63
19
E; s 7: 3 i?
141
77
12
18 -15
15
7
63
7
191 -
is
67
5
28 130
107 24
El
55 34
34
65
20
Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Atginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia Reference
Proline
Glycine Alanine Valine Leucine Isoleucine
Amino acid
52.1 64.7 79.7 70.4 65.6 31.8 32.2 66.0 92.1 132.2 8.0 85.2 46.4 33.2 39.3 27.4 51.4 13
21”
69 77 81 75 38 89 89 90 104 65 22 7 42 29 19 41 52 14
22
64 92 81 66 49 53 94 100 104 66 20 8 32 45 25 43 57 _ 14
23
75.1 82.6 60.1 84.9 43.5 54.1 78.2 68.0 98.9 117.8 17.8 15.8 62.8 40.3 21.3 35.2 34.8 8.7 _ 15
24
91 6.5 50 102 32 21 121 61 93 177 5 75 56 11 15 16 11 I_ 16
25 32 54 3.5 104 48 12 126 45 90 159 0 ‘15 154 54 0 48 0 24 17
26
28 34 126 98 55 0 33 130 81 99 130 0 0 82 34 0 48 17 _ 17
29 30 85 56 % 13 43 116 102 69 176 0 26 70 14 0 26 54 23 17
30 40 124 73 65 0 27 139 6.5 88 131 0 24 76 29 15 48 25 34 17
31 68 125 59 125 6 21 51 37 47 235 0 20 55 104 11 17 17 --I’ 18
32
Residues per 1000 residues
2 (Continued)
58 36 108 128 68 66 109 87 13 9 27 36 54 86 38 49 48 67 233 202 0 0 24 37 48 67 106 55 13 16 14 25 14 24 28 -16 17 17
27
TABLE
34
60 105 111 83 70 49 112 82 13 38 28 48 56 91 39 57 49 99 240 134 0 9 2.5 16 49 64 109 34 13 17 14 38 14 26 trz -18 18 19
33 55 91 56 113 34 37 68 54 76 178 6 23 64 69 14 33 23 tiz 19
35 52 73 52 118 52 40 82 63 97 146 20 75 39 18 33 27 ti3 19
36 48 79 56 119 49 38 72 60 88 154 7 20 67 52 18 41 27 tr2 19
37 52 75 55 116 51 39 78 61 91 146 21 73 45 19 41 27 tF 19
38 59 61 57 121 59 36 93 71 116 127 11 72 33 16 43 19 6 16
39
49 57 53 119 53 42 88 70 114 124 12 73 35 21 46 34 10 16
40
129
118.6
56.7
39.7
80.2
65.2
106.7
acid
acid
Isoleucine
Proline
Serine
Threonine
Aspartic
Glutamic
21
34
25
16
16
50.4
30.3
6.4 -------
15
Tryptophan Amide ammonia
Reference
30
16
10
22
16
18
23
28
58 8
89
91
20
31 -10
33
53 16
20
32 -20
28
64 20
20
45 -21
52
51 12
103
Phenylalanine Tyrosine
56 8
88
98
52 10
87
33.3 23.0
15
13
75.9
10
Arginine Histidine
14
922
29
29
58 19
84
3 20
192
85
47
66
7 41
Lysine
12
146 _
75
64
44
14 46
20
18
8= 21
-
31
22
tr2 -
35
38
27
30
63
53
11
7
86 110
85
19
3
85 195
47
23
22 -23
27
22
40
101
8
8
84 111
114
90 75
84
68
64
28 106
46
43
45 69
143
82
73
62
51
24
22.3 -24
31.6
33.3
23.4
41.8
57.3
16.9 t?
_ 25
23
31
15
31
97
14 24
117 91
54
63.8 98.9 111.6
71
41
55
91
76
96
73
53
95.8
48.5
46.6
77.5
65.3
78.5
86.8
52
1000 residues
81
54
53
60
64
50
per
140 6
75
43
49
Residues
2 (Continued)
74
41
48
4
188 -
87
44
59
2 44
136
85
52
59
47
17.1
177 -
84
49
57
8 64
149
53
77
45
46
Methionine
198 _
100
27
46
14 42
136
65
75
50
45
6.0
200 -
104
29
57
14 36
128
51
103
50
44
Half-cystine
98
38
57
23 40
125
47
104
59
43
185 -
122.0
48
55.1
Valine Leucine
52
104
61.4
42
52.1
41”
AIanine
acid
Glycine
Amino
TABLE
25
23
35
18
30
106
12 24
109 93
47
72
39
53
87
76
100
76
54
26
94.3
12.6
41.6
14.1
21.6
60.8
17.8 14.6
78.0 89.6
61.8
46.1
65.5
56.0
79.1
74.9
90.6
80.7
55
26
86.8
19.4
31.3
10.8
29.9
106.7
23.2
109.0 87.9
38.4
47.7
33.5
56.3
89.6
75.3
87.3
66.8
56
-
.27
29.5 -=
31.1
15.9
45.2
21.0
16.0
3.6
28
--
-
37
46
6
59
50
41
57 65
130.3 126.5
68
50
46
56
132
73
118
%
58
83.3
58.0
47.1
38.3
75.0
80.9
106.9
93.2
57
25
25
35
47
28
23 -26
-
116 86 -
65
81
42
91
9
88
147
94
59
3.7 290
-
44.8 25.4
24.0
48.2
47.7
24.3
14.3
121.2
81.7
57.2
70.4
47.8
50.6
123.5
68.6
80.7
65.7
60a
Glutamic
48
39
36
Arginine
Histidine
Phenylalanine
-
-
29b
Tryptophan Amide ammonia
Reference
29d
25.0 IO.9
42.9
23.9
17 -2Qa
Tyrosine
43.9
58
44.8
9.3 20.4
8 21
122.0
79.1
51.5
74.5
51.6
Methionine Lysine
Half-cystine
acid
Aspartic
124
64
94
acid
Threonine
90
Se&e
54.9
37
Leucine
44
56 111
Valine
Proline
44.3 122.3
85
Alanine
Isoleucine
67.9
78
Glycine
77.3
6Oc
acid
6Ob”
Amino
30
-27
-
26
37
27
5.5
59
7 20
156
99
49
58
42
43
59 119
84
60
61
31
25.3 -
25.4 43.6
49.5
13.8 54.5
-
117.0
84.0
57.5
87.8
50.0
53.3
116.0
72.0
80.7
66.5
62
32
24.0 PQ
27.0 50.0
51.0
21.0 50.0
5.0
139.0
83.0
52.0
63.0
56.0
48.0
116.0
64.0
81.0
68.0
63
33
21 -
21 35
51
19 58
12
162
97
57
72
45
41
98
65
73
63
64
34a
27.9 -2 -
31.4 44.1
48.5
17.0 52.6
10.0
127.5
89.9
57.8
75.2
50.6
34.5
114.6
62.6
90.7
70.3
65
24.2 -
39.3 53.8
39.8
15.5 60.2
9.8
110.6
94.4
51.6
76.6
39.1
31.9
69.4 114.7
97.3
71.9
46
34b
34a
96.0
60.2
85.1
65.9
42.5
68.7 93.1
72.0
74.7
66a
per
34b
24.5 -J-
18.5 41.9
46.0
17.1 56.3
-
120.4
Residues
2 (Continued)
--_c_--T.....----
22 -zQa
21 36
49
14 51
136 -
%
55
80
61
43
58 116
76
61
6%
TABLE
46 24
90
85
35
12 -30
-
-
120
91
64
66
67
51
75 83
83
79
67
38
26.3 -31
21.8 46.4
48.6
14.0 70.1
7.7
115
92.4
55.7
95.1
51.5
45.0
57.0 95.3
73.1
95.1
68a
1000 residues
38
27.9 -32
21.8 40.9
50.4
16.5 75.5
10.7
113
97.2
56.7
80.7
51.0
44.4
60.1 98.4
76.0
79.0
68b
-3 39
18
16 28
47
14 2.5
22
95
67
36
52
73
29
38 59
65
224
69
40
19.3 -34
16.1 30.3
49.2
17.6 28.6
20.7
96.3
71.8
38.7
47.5
60.9
34.8
40.5 78.9
65.9
194.0
70
40
11.0 -35
7.7 20.7
45.6
10.8 23.7
7.8
81.5
56.9
24.8
39.6
91.4
22.7
31.9 44.3
89.1
280.9
71
41
14.7 -36
16.9 30.1
41.4
14.6 14.6
17.2
86.7
57.7
32.5
45.7
79.0
33.7
36.6 66.6
53.1
225.4
72
42
15.3 -3
14.2 24.9
38.0
13.2 19.5
22.8
98.3
67.7
36.7
48.9
57.9
31.3
35.6 65.3
59.8
221
73
64.9 43
2.038
15.4
15.4 26.3
47.1
12.7 28.8
21.0
86.7
64.6
34.1
50.8
79.4
28.3
37.4 54.8
68.9
220.9
74
44a
-39
20.5
28.3
48.3 18.7
7.0 26.4
22.0
101.3
70.0
40.3
64.1 54.2
28.6
36.0 60.3
58.6
225.2
75
-
29.5
66.0
54.5
41.5
72.0
98.0
20.0
7.5 27.0
50.5 18.5
28.0
23.0
-41
28.1
69.8
49.0
40.5
70.0
97.0
22.7
5.0 26.0
48.2 14.4
26.8
22.0
-40
44a
38.0 59.0
36.0 60.2
45
60.0
65.0
-__-_---
220.0
229.0
Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia Reference
77
76'
Amino acid
44a
-42
17.0
19.0
44b
-4%
20
29
50 20
11.0
40.0
52.6 21.0
-
26
-
101
100.0
20.4
74
43
57
68
31
37 70
60
207
78a
70.0
45.5
62.8
62.0
30.0
43.0 60.0
67.0
200.0
78
44b
-42b
22
30
46 17
36
-
-
106
79
54
66
83
27
42 70
58
170
78b
46
-43
16.8
27.9
50.8 17.4
26.6
13.8
22.0
91.6
65.6
40.7
51.8
77.1
30.0
36.6 57.3
65.2
212.4
79
47
-44
32.8
45.9
55.7 26.2
59.0
124.6 22.9
91.8
52.5
72.1
59.0
39.3
62.3 104.9
75.4
75.4
80
TABLE
48
-45
24
33
56 28
73
131 11 15
95
54
85
50
46
58 87
83
78
81
31.4 49
22.4 49
-
39.5
57.6
41.9
20.1 49
-
41.2
64.2
39.5
65.8
7.9
68.6
7.6
28.6 62.6
107.7
35.4
58.9
106.0 76.9
58.0
70.4
61
39
71
69
24
39 28
62
80
84
76
50
120
35
17
34 17
68
85
85
95
13
90
85
3
17 4
93
67
86
50
41
115
54
9
24 4
89
%
87
97.2
53.4
67.6
39.6
38.8
57.4 68.0
91.0
211.9
88
50
-46
45.4
53.2
12.0
25.7
61.5
20.0
17
16
16
-
51
7
8
30
28
-
_ 52
0
8
4
8
-
51
0
0
17
45
51
-4'7
-
-
-
28
129 127 100 104
4
6.9
54a
-
68.0
20.9
11.7
23.6
64.3
14.0
87.5 59 60 38 40 123.0 1.8 262 290 316 332 -
121.5
72.9
68.2
33.2
44.1 28.6
69.5 97.2
85.6
74.4
83
72.8 119.2
56.0
45.0
82~
119.7 124.8 -
92.2
31.2
62.1
26.5
42.3
67.3 108.2
53.2
45.2
82b
68.1
87.4
98.7 29.1
86.6
27.8
85.6
37.4
28.7
49.5 112.2
55.3
52.8
82a
Residues per 1000 residues
2 (Continued)
54b
-
_
20.8
40.8
23.6
40.0
60.4
13.7
131.9 13.1
104.5
56.5
56.5
44.8
56.4
76.5 108.0
88.8
72.2
88a
103
38
77
29
1
27 30
18
153
90
32
55
38
25
26
29
41
-
-
-
-
55
24
38
17
26
34
36
121 132 177 219
125
38
81
27
6
38 29
26
142
89
3
ti
Is 3
g
F F! g
G
5
El
Reference
Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amideammonia
Amino acid
92
88.0 197 83.2 145 65.0 66 71.7 11 39.9 29 56.1 54 66.9 233 66.2 136 116.9 19 120.8 57 4.6 0 14.2 0 58.4 10 47.3 27 23.4 4 38.4 0 23.5 6 4% _ _ 57 56
91a
184 131 72 16 34 54 212 124 27 63 8 2 14 27 5 9 20 -_-__ 57
93
218 100 50 43 21 90 110 128 40 62 18 5 20 50 13 26 12 -
58
58
95
196 149 75 12 30 77 199 128 22 67 11 2 12 3 3 6 6 -
94
97
177 122 67 4 16 111 201 153 21 58 tiL 1 6 43 2 4 tr 59 58
255 113 49 38 9 95 110 140 24 54 12 2 10 50 12 22 6 -49
% 99 51 54 47 40 59 115 115 133 83 50 8 46 34 12 25 32 58
98 198 136 60 52 13 % 175 148 17 53 0 0 3 36 0 16 tr -58
99
TABLE
86.9 86.3 53.8 64.3 25.7 76.2 160.1 124.6 83.2 86.1 ti2 41.9 34.9 30.0 31.4 14.4 62
105
158 68 147 86 85 71.8 113 95 106 115 99 93.8 55.6 71 86 63 111 79 45 41 56 36 38 65.6 29 16 21 28 43 20.3 97 99 119 135 80 84.8 143 113 101 157 177 131.0 117 241 95 183 181 195.6 46 47 66 32 66 61.1 65 74.3 62 70 101 62 27 23 tP 14.7 0 14 tiL tr* 20 18 37 17 33 40.1 38 34 40 14 16 25.6 4 14 13 10 12 22.6 24 14 20 8 16 25.0 8 11 1s 4 11 17.9 -50 -5% -58 58 58 60 61 61 62
110 104 67 57 31 64 148 126 73 84 0 0 38 37 11 36 14 -
104
107
100 101 102 103
106
Residues per 1000 residues
2 (Continued)
109
110
88.3 73.9 69.2 49.7 98.1 104.9 45.3 41.0 39.4 27.3 49.1 47.3 32.8 21.6 23.6 146.1 95.8 90.0 117.6 162.2 133.7 319.3 270.1 335.8 41.3 29.9 20.5 52.2 45.7 38.1 7.1 20.6 24.2 27.0 11.7 28.7 29.7 16.7 26.8 29.4 11.2 22.1 11.4 12.6 10.6 62 63 63
108
%.6 90.9 60.0 73.5 32.7 68.9 113.5 125.3 77.7 93.2 8.6 41.8 40.1 20.5 31.0 25.3 63
111
Fi
% 5
g 2 s m
t? $ 2 g
b 6
$ o
109.7
139.2
90.2
acid
acid
Setine
Threonine
Aspartic
Glutamic
10.1
11.0
52.0
49.8 8.6 %.6
64
Phenylalanine
Tyrosine
Tryptophan Amide ammonia
Reference
33
Lysine
Histidine
24.1
Methionine
Arginine
4.3
Half-cystine
74.6
39.7
45.1
57.0
Leucine
Proline
66.6
Valine
Isoleucine
92.0
105.1
112a
Alanine
acid
Glycine
Amino
64
38.2 115.5
36.5
11.2
12.0
36
12.2
-
79.0
91.5
155.0
140.5
45.5
36.3
47.3
57.1
99.3
101.3
113
_
65
27 12
66
31
46
60
14
20
73
56
65
89
41
44
95
61
9.5
106
114
65
30 17 -
70
27
38
56
14
17
77
57
67
74
41
47
100
70
99
100
115
-
65
27 15
59
31
49
61
13
17
78
58
63
92
45
42
94
57
98
102
116
-
65
26 14
60
31
49
61
13
21
76
59
63
88
43
39
91
54
99
106
117
65
23 10
50
31
60
63
15
18
97
70
54
98
44
39
89
50
95
97
118
66
28
66
29
45
60
17
16
77
58
66
101
42
45
93
62
93
103
119
TABLE
66
27
64
29
43
64
16
12
82
60
69
103
42
43
94
64
92
98
120
_ 66
29
60
24
38
57
11
10
79
61
71
110
39
45
94
65
%
106
121
Residues
2 (Continued)
66
_
29
62
27
41
60
14
15
84
65
67
101
43
45
95
65
93
97
122.
per
82
67a
-
22
49
60
100
-
-
66
71
43
%
69
15
70
23
91
142
123
45
54
90
81
67a
22 -52 _
-
-
76
76
46
95
78
22
61
20
90
146
124
1000 residues
67b
_
23
48
59
110
78
12
0
66
67
40
95
76
16
57
15
87
149
124a
68
27 -53 -
36
23
46
86
17
0
103
83
57
68
34
54
89
97
91
103
125
68
17 -54 _
29
24
22
67
2
0
93
73
42
57
25
34
53
96
70
82
126
68
13 -55 -
50
50
26
122
10
0
147
86
40
60
40
37
93
79
89
62
127
68
26 -56 -
44
34
34
92
15
13
103
107
54
54
43
39
99
72
95
76
128
68
18 -57
56
47
26
87
15
7
88
102
48
59
34
15
115
87
119
76
129
68
15 -53
44
89
68
32 -53
33
27
20
8 165
21 121 14
0
122
88
42 20 80
54
34 65
66
135
131
0
109
81
21 38 34
33
59 116
117
87
130
5 $
z
is
7;: s g
z
E-
8
5
acid
Glutamic
7.6 31.5
-
Tyrosine
Amide
Reference
-
-
Tryptophan
69
13
Phenylalanine
ammonia
56.8 13.9 -
62
Histidine
70
-
42.5 17.1
103
116.1
143.0
151
23
52.5 101.0
74.2 17.3
49 141
46 36
31 9
Arginine
Lysine
Methionine
Half-cystine
acid
Aspartic
Threonine
Serine
Prolirie
Isoleucine
Leucine
69.4 53.0
97.3 45.4
Alanine
66 44
61.0
80
98 49
Glycine
Valine
133
acid
132”
Amino
70
-
85.0 12.7 -
41.5 16.4
114.0
3.5 31.1
141.0
54.0 133.0
53.0 20.0
56.0 37.0
81.0 58.8
62.0
134
71
124.8
31.8 18.6 3.7
49.8 16.4
126.8
9.4 24.0
172.2
51.1 102.5
30.2 40.5
101.1 46.8
86.4 43.4
45.3
135
71
142.9
33.0 19.2 3.8
54.7 17.8
124.7
6.7 24.6
177.1
55.2 94.9
23.5 43.5
101.3 48.6
79.4 46.5
45.5
136
71
175.0
34.9 19.2 3.7
53.0 21.4
99.5
7.8 23.6
191.1
51.0 98.1
23.1 46.9
93.5 50.2
90.9 50.6
51.3
137
72
-
18 -
36.5
55 19
104.5
13 20
195
49.5 102
25 46
105 49
87 43
43
138
72
-
17 -
33
62 17
104.5
28
205
50 99
19 44
109 40
86 44.5
39
139
TABLE
72
-
26.5 -
34.6
59.2 28.2
76.5
14.2
115.3
55.9 105.1
51.9 69.5
83.4 48.6
82.7 63.6
86.0
140
Residues
72
-
29.3 -
32.2
46.3 32.1
73.7
14.2
110.9
46.3 128.6
49.1 82.3
84.0 21.8
98.3 33.1
119.1
141
per
2 (Continued)
8.6
73a
-
20.1 -5s
27.6
61.2 19.6
104.3
-
130.9
53.7 100.0
21.3 78.6
88.9 39.0
89.4 59.7
94.7
142a
73e
-
32.6 -
39.6
58.9 25.2
60.4
19.2
121.6
38.1 102.8
64.9 43.8
67.9 41.3
67.3 61.0
152.8
142b
1000 residues
73c
-
32.3 -
36.4
70.8 24.1
67.2
20.0
122.6
49.1 95.5
51.4 53.3
89.0 52.2
75.5 63.1
96.2
142~
-
-3 74
75
29
39
19 11
35
76 510
70
66 125
19 167
14 50
32 46
191
144
21--
20
30
207 16
61
71 135
92
46 97
38 36
66 34
83 61
69
143
75
68 -60
26
8 8
55
0.2
44
40 74
151 52
69 24
158 65
131
145
7s
12 -61
28 0.4 54
2
9 4
49
14 83
1108
25 15
231 16
338
146
171
57 130
71 144
43 25
66 39
103
148
31 65 4
-75
15
212774 60 25 -32 -a
22 49
38
2831 10 10
73
43 116
107 98
51 20
106 40
120
147
75
11 -@
9 0.2
39
4 2
29
16 47
50 2.5
110 64
30 78
411
149
75
20 10 -65
8 IO
26
24 24
113
62 150
63 85
92 47
102 61
105
1.50
s
-
3 x
;;:
-CI ;d 0
0
5 g
ti
b Ej
iz 2o
128
126 2
68
116
38
125
121 4
Isoleucine
Proline Setine
Threonine
Aspartic Glutamic
75
-
ammonia
Amide
Reference
16
-a
Tyrosine Tryptophan
1
Histidine
35
21 23
Lysine Arginine
Phenylalanine
12
Methionine
Half-cystine
90
42
Leucine
acid acid
49
69 81
-
9
75
-67
22
4
29 74
15
56
46
85
76
82
Valine
107
117
100
152
151”
Glycine
acid
Alanine
Amino
-
75
-68
14
19
6
26 25
19
114 15
132
57
88
90
36
75
40
81
159
153
-
-69
75
34 12
1
24 64
6
9
64
147
20
116
37
37 15
35
215
169
154
-
75
7 12 -70
6
43 33
12
21
105
171
47
123
61
38
68 77
74
102
155
-
75
20 17 -71
10
27 1
27
13
97
119
50
85
167
33
59 53
76
144
156
-
-
-
75
14 1
13 14
3
26
119
152
62
88
97
38
54 56
61
201
157
_ 75
18 3 -72
6
41 42
15
28
97
139
83
77
36
72 52
72
82
135
158
TABLE
-
15
17 4
2
21 21
33
16
110
136
68
95
52
75 43
66
82
159
159
_ 75
33 9 -73
4
15 38
11
14
129
113
94
72
70
123 29
46
100
101
160
Residues
15
32 -74
30
3
36 68
16
67 8
273
42
76
67
30 19
24
69
141
161
per
2 (Continued)
75
13 -75
22
27
62 48
23
109 11
85
113 62
60
79 32
42
114
98
162
15
41 19 -76
15
16 7
21
102 6
119
78 59
111
81 39
60
104
122
163
1000 residues
15
31 22 17
19
37 39
23
99 18
132
86 63
91
72 26
54
86
96
164
15
51 -78
75
-79
33
30
89 7 14
29
24
6
0.4
59
164
110 22
41
26 15
25
144
200
166
107 5
10
%
63
101
97 54
95
15 24
54
46
141
165
75
42 -80
17
15 1
25
3
3
69
143
74 23
39
50 15
38
62
380
167
_ 75
12 -81
36
5
41
42
30
4
121
113
61
93
68
31
56 89
90
109
168
75
14 -82
33
6
25
33
30
14
114
142
72
63
53
36
83
62
114
108
169
-
-= 75
33 4
5
35
34
11
11
109
141
57
83
21
41
77
61
120
158
170
-
75
-
62 -84
34
2
22 12
Is
33 1 0.4
i
3
5 7: E z
a’
z
g
25 10 104
55
5
35
64
187
348
171
30 11
94
50
13
159
38
97
acid
acid
Leucine
Isoleucine Probe
Set-me
Threonine
Aspartic
Glutamic Half-cystine
8
Reference
Tryptophan Amide ammonia
-
75
-
22 -89
12
~enylal~ine
-85
6
Histidine
Tyrosine
35
27
At&nine
75
83 37
64
21
Lysine
24
9
103 3
119
45
81
43
Methionine
61 15
58
38
81
Valine
126
190
200
173
172”
Glycine
acid
Alanine
Amino
-
75
23 -87
44
67 16
36
26
114 2
103
50
70
23 85
68
48
108
116
174
-
75
30 -88
72
57 7
15
-
7.5
-89
19
28
13 8
20
20
15
1
103
0.7
116
63
66
62
55
101
71
81
160
176
42
80
12
47
55
6
52
40
142
335
175
-
75
13 -3
40
17 0.6
11
7
3
117
133
58
91
69
40
63
60
143
91
177
65
75
-----
-
56
48 35
82
10
21
91
99
56
61
59
37
56
61
88
114
I78
6
75
-pl
12
14 2
21
12
18
94
90
47
141
61
19
69
40
176
179
179
TABLE
7
75
-91
14
11 7
39
13
17
86
117
48
121
55
25
74
42
161
163
180
2
75
41
13
10 6
37
10
8
105
125
63
145
22
35
71
60
141
145
181
Residues
75
10 -70
20
-
-3 75
7
15
8 4
17
17
16
84
110
44
103
93
25
71
42
163 181
183
75
15 -93
74
45 1
34
30
103 16
133
46
58
82
35
76
63
116 74
184
1000 residues
14 2
23
28
20
91
100
47
119
92
26
74
39
89
203
182
per
2 (Continued)
75
-
28 -3
16
6 0.2
12
1
9 4
11
11
37
57
50
121
83
19
526
185
-
11
75
-95
13
53 14
30
12
104 8
120
67
104
95
23
70
34
150 92
186
-
6
75
-M
17
2
14
15
59
21
105
117
58
106
113
17
100
26
140 89
187
75
11 -97
17
18 3
27
24
113 23
143
59
97
130
30
80
36
71
118
188
-
5
75
-98
36
44 4
39
20
12
111
117
61
65
53
44
%
62
108
121
189
75
46 -99
95
9
6
15
11
26 8
48
11
34
54
26
59
17
519 16
190
75
0.5 -1QQ
6
2
4
28
4
10
53
308
17
213
11
11
22
19
227 63
191
75
9 0.4 -101
1
2
13
19
10
62
286
21
207
25
15
27
16
64
222
192
Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia Reference
Amino acid
279 54 40 32 23 78 34 24 142 32 9 14 36 92 15 41 55 75
151 61 51 53 39 12 52 40 122 86 16 29 66 94 14 35 19 _ 75
156 64 60 61 43 71 67 43 153 96 41 8 34 39 10 40 14 -102 75
193” 194 195
1.52 70 41 49 36 64 72 49 108 85 43 21 51 72 23 44 20 _ 75
1%
198
199 207 55 62 34 32 112 54 59 120 84 104 29 16 7 2 20 5 _ _ 75
204
205
206
207
208
209
210
211 212
213
165 370 378 530 482 355 136 353 284 305 274 323 60 50 158 36 43 64 61 47 79 58 51 65 61 26 19 28 32 47 33 37 41 34 37 50 36 37 36 33 27 24 41 33 41 32 31 37 31 20 22 17 18 15 23 22 24 18 17 24 114 27 22 41 49 74 119 64 56 73 79 69 60 85 97 41 48 49 73 41 48 48 48 35 60 29 10 21 26 38 51 25 29 30 32 22 127 143 34 48 60 117 148 152 177 211 246 160 90 67 27 37 46 49 72 41 56 44 43 32 101 26 2 23 17 28 21 22 15 16 22 38 14 23 62 77 11 13 34 32 21 26 23 24 43 17 13 4 41 87 19 26 21 19 22 11 106 59 24 4 53 31 23 30 32 27 11 1 1 1 0.2 0.3 5 1 16 11 7 6 9 14 54 53 24 32 26 36 26 34 27 24 45 7 2 39 14 44 15 47 46 11 24 24 54 ~107 -108 -109 -110 -111 -112 -113 -114 -115 _ _ -116 _ _ 75 75 75 75 75 75 75 75 75 75 75 75
203
Residues per 1000 residues
2 (Continued)
200 201 202
138 143 248 318 72 98 60 46 42 39 31 17 57 36 32 19 39 25 14 5 70 156 84 43 124 82 81 1% 46 75 35 12 141 114 215 190 116 89 62 34 26 2 10 10 19 17 12 4 18 26 30 27 32 20 13 23 7 7 7 9 40 38 20 13 10 35 47 36 -tm -104 -105 -106 _ 75 75 75 75
197
TABLE
338 57 43 31 23 54 47 24 201 37 12 42 11 11 5 37 29 _ 75
214
40
31
129
40
35
36
70
38
21
198
38
10
23
Serine
Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine
Reference
-
25
21
ammonia
38
32
Amide
45
36
-
58
62
Tryptophan
303
301
Glycine
Alanine Valine Leucine Isoleucine Proline
23
41
7.5
36
3
70
-
7.5
-117
36
58 9
14
23
58
216
21Y
Amino acid
11
27
52 14
27
16
18
44
252
25
69
53
22
33
25
56
256
218
-
75
-
75
-..m1IH -119
4
25
62 19
45
35
22
53
214
39
55
59
19
30
19
48
252
217
7s
_
-120
61
36
1
34
19
38
8
37
173
IS
40
60
15
27
29
45
367
219
-
19
75
_
35
33
59
32
16
4s
46
131
32
91
37
43
5.5
58
59
211
220
-
75
-121
20
17
5
24
18
6
11
38
112
16
98
14
16
48
27
241
289
221
28
-
75
-122
20
17
5
25
18
6
11
41
118
7.5
-
-123
0.3
28
7
43
14
19
5
42
76
126 15
15 98 17
15
38
16
171
352
223
18
48
29
216
291
222
TABLE
-
75
-124
48 4
27 11
19
13 20
36
69
16
73
75
-
-125
44 0.3
7 0.3
7
3 9
38
84
23
65
46
13
25
33
12
27
127
475
225
33
20
120
453
224
4 -
75
_
75
-127
10 -126
36
30 4
20
12 18
36
72
17
63
28
8
33
17
144
461
227
45
40 10
22
9 17
44
69
20
58
38
12
39
23
97
454
226
-
75
-12R
88
69
46 8
22
1 23
3.5
41
20
60
6
20
24
14
46
475
228
Residues per 1000 residues
2 (Conrimed)
-
75
-12Y
72
40
28 1
16
14 57
73
86
37
51
58
37
47
44
54
283
229
_
2
75
-13"
24
89 19
56
21 7
62
252
43
67
80
21
33
35
63
125
230
-
4
75
-131
33
49 4
33
19 3
52
321
35
51
-
3
75
-132
28
51 5
35
20 3
52
327
45
52
55
18 23
21 25 58
39
37
206
232
36
39
217
231
-
75
-133
27
37
36 2
30
8 13
85
224
45
89
81
44 30
32
86
132
233
-
75
-134
27
27
9 3
26
6 21
70
93
75
__
-135
18
31
3
26
14
7 17
77
88
111 35 101
98
27 12
30
61
341
235
102 33
36 14
29
58
349
234
75
_
-136
20
31
12
60
19
13 II
63
66 48 194
93
31 14
51
56
214
236
Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia Reference
Amino acid
Residues per 1000 residues
2 (Continued)
211 58 51 32 12 100 62 4.5 197 64 13 10 18 61 11 32 20 -131 1.5 136 2 81 29 27 5 22 5
76
76
22 48 89 100 110
115 86 43 79
I19 6 30 34 40 8 33 20
135 84 53 97
113 125 67 135 24 2 64 29 29 57 18 23 19 26 28 23 33 29 6 I1 4 4 38 32 27 14 26 12 17 2 -------------_-____-__I-------------_---_-_I76 76 76 76
30 92 89 53 88
152 107 44 62
32 67 82 63 100
26 76 80 69 127
34 62 80 63 121
195 89 45 78
27 115 101 54 99
115 107 50 70
140 80 53 79
-
76
24 28 32 4 35 47
98
46 62 67 50 %
222 66 38 83
76
135 93 18 12 15 21 2
20 91 94 45 117
153 85 38 55
76
94 6 17 33 37 17 41 35
54 49 60 43 95
216 63 54 88
76
116 % 28 38 18 20 10
22 38 88 60 106
183 76 34 61
76
53 32 30 18 7 77 76
41 61 35 29 57
341 60 40 44
76
116 42 24 22 8 19 12
26 72 81 59 87
77
77
86 103 20 10 10 10 79 34 46 6 33 42 56 28 65 52
29 86 80 21 75
39 58 57 22 75
16 66 77 20 %
41 25 77 33 89
20 25 58 24 86
33 59 64 31 60
31 45 34 16 44
77
77
77
77
77
77
77
77
97 124 136 104 109 157 145 150 17 17 22 11 26 34 44 16 22 17 11 12 29 12 21 18 36 61 65 37 42 35 59 58 7 3 29 22 0 11 6 4 28 29 22 24 21 33 40 42 39 32 32 18 44 24 46 32 22 28 17 9 17 19 16 25
36 29 29 51 90 79 60 62 70 55 44 32 95 118 108
182 111 105 122 126 147 181 130 187 120 170 123 85 101 121 93 108 157 115 155 89 161 51 59 56 59 57 49 39 58 41 51 57 78 53 40 52 47 61 33 58 36 50 45
231a 238a 238b 239a 239b 240a 240b 241a 241b 242a 242b 243a 243b 244 245 246 247 248 249 250 251 252 253
TABLE
iz .3 5 $
F U ir 3” B jq
8z
Glycine Alanine Valine Leucine Isoieucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia Reference
Amino acid
255
256
257
127 177 74 91 104 74.3 101 89 41.9 43.9 73 71 52.7 39.5 90 93 31.8 28.3 57 48 84.0 85.1 4.5 37 81.3 80.9 112 120 53.0 57.4 33 52 148 163 to9 118 134 161 130 141 4.7 6.4 2 2 5.7 7 5 15.0 50.1 31.5 19 23 36.0 31.1 39 21 49.0 29.6 1 20.4 18.8 40 31 12.5 8.5 12 12 -138 -139 ----18 78 75 75
254a
259
72 89 66 loo 57 38 73 72 132 137 7 10 38 45 8 33 14 -140 75 75
73 79 68 104 68 31 105 55 13.5 115 1 5 35 30 42 49 8 _
258 669 21 11 12 21 25 23 5 16 13 14 20 19 33 6 13 70 -141 75
260
262 286 79 50 43 29 48 65 54 105 68 8 3 38 61 10 34 12 -144 75
264a 264b
510 333 38 61 43 49 27 42 16 29 24 47 60 54 19 47 52 91 15 58 2 10 3 3 15 37 46 59 12 9 21 34 97 30 -193 -144 75 75
263
Residues per 1000 residues
2 (Continued)
626 435 28 53 12 32 28 34 10 34 23 51 17 40 8 22 23 74 12 36 5 22 34 64 13 16 17 46 21 1 29 42 93 9 -142 75 75
261
TABLE
571 49 53 12 5 54 26 25 IO 15 7 27 14 6 I 82 44 75
547 54 57 10 4 54 28 24 7 13 7 19 24 18 4 84 39 75
266a 2661, 266~
494 550 41 42 42 34 21 16 27 8 54 37 89 20 II 23 29 23 19 24 4 0.4 72 60 13 24 13 2.5 3 3 54 41 12 69 -143 -130 75 75
265 648 17 18 6 5 34 29 9 32 9 4 17 20 38 4 85 13 75
269
661 132 64 18 46 45 16 49 63 41 58 6 5 28 46 32 74 51 26 67 76 9 48 75 35 224 100 9 101 100 4 38 79 17 3 16 22 17 61 34 35 29 4 21 86 19 39 13 12 32 3614Q . --75 75 79
267a 267b 268
Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia Reference
Amino acid
271
272
273
68 70 72 79.6 46 49 56 50.6 64 76 73 82.5 61 63 68 94.6 46 55 52 53.0 58 46 57 55.8 76 48 71 74.1 72 63 72 42.6 110 113 118 86.2 108 115 87 107.2 83 8.0rS3 78 70 16 18 19 3.1 56 60 40 55.4 18 43.2 34 29 20 20 13 21.2 40 41 48 49.0 37 54.1 34 36 12’50 18 16 3.7 -151 -152 _ 79 80 79 n
270”
70.8 92.3 76.2 63.8 24.7 61.7 98.5 100.8 74.0 158.3 2.6 15.5 36.0 36.2 21.5 60.0 7.0 -1% 81
274
276
22 18 122 141 43 41 121 135 34 33 50 43 42 47 131 145 211 206 15 10 74 69 101 87 6 4 8 5 21 17 80 80
275 67.5 88.8 84.1 98.5 52.0 47.6 52.3 29.7 95.4 116.0 20.6 66.8 41.8 23.1 36.4 29.7 81
36 39 21 17 9 19 536 22 67 48 0 3 75 44 53 6 5 _ 82
278 83 75 48 78 41 72 69 74 112 97 17 23 34 43 20 51 45 17 _ 83
106 78 70 66 55 34 82 75 129 84 10 8 40 52 18 46 34 13 _ 84
279 -280
282
164 326 67 127 40 23 92 28 35 I1 14 122 111 25 40 18 91 36 141 73 6 4 13 51 18 61 48 6 10 36 15 28 -1.55 _ 85 86
281
Residues per 1000 residues
2 (Continued)-
277
TABLE
39.1 15.7 26.3 30.6 148.5 89.8 9.0 13.6 64.3 42.8 7.4 49.2 43.0 190.4 -157 87
14 208 25 22 51 79 5 39 45 4 13 -15.5 86
-
53.9 72.0 49.4 55.0
284
313 119 24 30
283
75.4 8.1 12.7 40.0 53.1 9.0 37.6 20.4 22.9 _ 88
47.3 40.7 68.3 58.4 113.8
84.1 153.3 84.4 70.5
285
115.8 0 19.8 80.8 52.3 !.I.4 23.6 11.2 3.7 89
47.4 36.6 73.2 61.0 95.6
78.3 128.0 84.5 91.2
286
151 14.5 85.2 25.0 12.6 28.1 22.1 90
64.9 26.2 42.3 48.0 126
52.0 109 84.3 108
287
145 13.5 83.8 25.2 13.3 27.6 23.4 90
66.2 26.2 44.0 48.8 126
52.0 115 84.0 106
288
: tl .g z H Fi Is 5
E3
n Protein number corresponds to that given in Table 1. I Not reported (--). * tr, Trace. 3 The amino acid analyses of free secretory piece is in Ref. (2) and is similar to that of the bound material. Carbohydrate content of free secretory piece expressed as a percentage: gafactose, 3.12; mannose, 3.95; fucose, 2.26; hexosamine, 4.36; sialic acid, 1.9. 4 No hydroxyproline detected. ’ See also Ref. (5) for analysis of pooled IgG. B Carbohydrate residues, percentage: hexoses, 5.0; fucose, O.t;acetylhexosamines, 3.6; sialic acid, 3.4 ’ Carbohydrate residues, percentage: hexoses, 9.9; fucose. 0.7; acetylhexosamines, 7.4: sialic acid, 3.4. 8 Carbohydrate residues, percentage: hexoses, 3.1; fucose, 0. I; acetylhexosamines, 3.2; sialic acid, 2.0. 9 Carbohydrate residues, percentage: hexoses, 6.2: acetylhexosamines. 4.1; sialic acid, 3.1. lo Carbohydrate residues, percentage: hexoses, 10.8; fucose. 0.4; acetylhexosamines, 9.2; sialic acid, 14.3. I’ Carbohydrate residues, percentage: hexoses, 3.2; fucose. 0. I; acetylhexosamines, 2.7; sialic acid, 1.7. See also Ref. (8). ‘* ~-Acetylglucosamine, 8.2%. I3 Glucosamine, 3.7%. In Ref. (IO), the amino acid analyses of the inhibitor dimer and the monomer and dimer isolated from deproteinized plasma are also given. I4 In Ref. (II), the amino acid analyses of fractions obtained by treating SCMK-A with different proteases may be found. r5 In Ref. (l2), the amino acid analyses of fractions obtained by treating a-keratose with different proteases may be found. I6 Less than 10 residues. In addition to these electrophoretic bands (Nos. 26-31). the analyses of two more DEAE functions are given in Ref. (17). I7 This result is the mean value of the analyses ot two samples from two patients. r” Analyses of VLDL subfractions are also given in Ref. (19). Is Composition of constituents corresponding to 100 mg of proteins: I .3 mg of phospholipid and 1.2 mg of hexoses. *OComposition of constituents corresponding to 100 mg of protein: 34 mg of protein, 0.9 mg of phospholipid, and 0.78 mg of hexoses. 2’ Composition of constituents corresponding to 100 mg of protein: 60 mg of protein, 0.4 mg of phospholipid. and 0.43 mg of hexoses. *2 Amino acid composition of electrofocused fractions also given in Tables 7 and 8 of Ref. (21). 23This is the analysis of preparation 310. The analyses of other preparations are given in Table 3 of Ref. (23). 24Carbohydrate composition (g/l00 g of protein): glucosamine. 2.49; total hexose, 6.00; glucose, 2.24: galactose, 2.25; mannose, 1.51: fucose, trace; sialic acid, 2.55. 25 The amino acid analysis of the outer layer is given in Table 2 of Ref. (27). 26 Amino acid analyses of a red pellet and colorless supernatant given in Table 2 of Ref. (28). 26a Amino acid analysis of lipid-extracted membrane (29c,d). 27 Amino acid analyses of the protein precipitated at pH 4.5 and of the protein soluble at pH 4.5 can be found in Table 2 of Ref. (31). 28 Amino acid analyses of water layer after butanol and pentanol extraction can be found in Ref. (32a). Additional amino acid analyses of membrane fractions can be found in Ref. (32b). *9 Glucosamine, 1.74 pmol. 29aThere are 2.1 mol% glucosamine and 0.5 mol% galactosamine. All resuhs are based on IO0 residues of amino acids plus amino sugars. 2YbThere are 1.12 mol% glucosamine and 0.50 mol% ~lactosamine. All results based on I00 residues of amino acids plus amino sugars. 3o Amino acid analyses of five fractions of fat soluble membrane from :
% s 2 ; z
b E; h sz 2 i
3
G
milk have been reported in Ref. (36) and of other fat globule membrane 3RAlso found were 81.1 residues of hydmxyproline, 21.3 residues of hydroxylysine, 15.8 residues of glucose, 18.3 residues of galactose, 4.32 proteins in (37). 31~arbohydmte composition (nmokmg of protein): fucose, 16.4; residues of mannose, 0.98 residues of fucose, 7.40 residues of N-acetyl2.67 residues of mannose. 47.8; galactose, 94.0; glucosamine, 63.6; sialic acid, 13.9: glucosamine, 0.99 residues of N-acetylgalactosamine; N-acetylneumminic acid, and 16.13 residues of glycosylgalactosylglucose, 23 1. 32 Carbohydrate composition (nmokmg of protein): fucose, 31.1; hydroxylysine. Also reported are selected analyses of the diabetic human mannose, 92.4: galactose, 189; glucosamine, 138; sialic acid, 24.2; glomerular basement membrane. glucose, 306. 3g Also found were 24.5 residues of hydroxylysine, 12.0 residues of B There were also found three residues of 3-hydroxyproline. 67 residues 3-hydroxyproline, and 53 residues of 4-hydroxyproline. of 4-hydroxyproline, and 22 residues of hydroxylysine. Carbohydrate 4u Also found were 25.0 residues of hydroxylysine, 8.5 residues of composition (mg/lOO mg of protein): glucose, 2.6: galactose, 2.7; mannose, 3-hydroxyproline, and 56.5 residues of Chydroxyproline. 1.1; fucose, 0.45; hexosamine, 1.6; sialic acid, 1.05. Amino acid analyses *r Also found were 22.5 residues of hydroxylysine, 7.0 residues of of soluble and insoluble fractions, obtained by autoclaving at 110°C and 3-hydroxyproline, and 56.0 residues of 4-hydroxyproline. tritiated glomerular basement membranes are in Ref. (39). *P,Also found were 21.8 residues of hyd~xyfysine, 7.0 residues of 3* There were also found 8.6 residues of 3-hydmxyproline, 58.2 residues 3-hydroxyproline, and 50 residues of 4-hydroxyproline. of hydroxyproline, and 18.4 residues of hydroxylysine. Carbohydrate 42aThere are 25 residues of hydroxylysine, 26 residues of 3-hydroxycomposition (mg000 mg of protein): glucose, 1.6; galactose, 1.8; mannose, proline, and 58 residues of Ilhydroxyproline. 1.0; fucose, 0.45; hexosamine, 1.25; glucosamine, 0.90; galactosamine, 42bThere are 17 residues of hydroxylysine, 27 residues of 3-hydroxy0.29: neuraminic acids, 0.51; glycolyl, 0.38; acetyl, 0.13. proline, and 50 residues of 4-hydroxyproline. 35There were also found 3.3 residues of 3-hydroxyproline, 87.8 residues of 43 Also found were 77.1 residues of hydroxyproline, 21.8 residues of and 13.4 residues of hydroxylysine. Carbohydrate hydroxyproline, hydroxylysine, 17.1 residues of glucose, 22.1 residues of galactose, 5.5 composition (mg1100 mg of protein): giucose, 2.5; galactose, 2.9; mannose, residues of mannose, 1.0 residue of fucose, 12.0 residues of hexosamines, 1.1; fucose, 0.5: hexosamines, 1.40; glucosamine, 1.20; galactosamine, and 2.6 residues of sialic acids. In Table 2 of Ref. (46) is also found the 0.30; neuraminic acids, 1.05; glycolyl, 0.80; acetyl, 0.25. amino acid and carbohydrate analyses of urea-extracted and SDS-extracted 3sThere were also found 18.4 residues of 3-hyd~xyp~line, 84.6 residues membranes. of 4-hydroxyproline, and 29.9 residues of hydroxylysine. The amino acid 44 In Table 1 of Ref. (47) is found the amino acid analyses of 16 fractions analyses of KCI, KBr, and sodium trichloroacetate extracts are given in obtained from the nuclear membrane. Table 1 of Ref. (41). 45 Also found (g/100 g): carbohydrate, 5.81; glucose, 2.11; galactose, 37 There were also found 22.2 residues of 3-hydroxyproline, 81.3 1.51; mannose, 0.82; fucose, 0.09; N-acetylglucosamine, 0.79; N-acetylresidues of 4-hydroxyproline, and 26.1 residues of hydroxylysine. Also found were (~mol/lOO mg) sialic acids, 2.99; glucosamine, 6.04; glucose, galactosamine, 0.19; sialic acid, 0.30; lipids, 24.00; phospholipid, 20.30; cholesterol, 3.70; RNA, 0.23; DNA, 0.09. 17.2; galactose, 18.5: fucose, 1.6; mannose, 3.5; and (g/100 g) phospho46 Also found were 21.5 residues of glucosamine and 56.4 residues of lipids, 2.05; cholesterol, 0.75. E 3 3 5 z
is E; ;4: ?$
;f; 00
a Hydroxylysine, 0.3 residues, 58 &g of glucosamine, 26 pdg of galactosamine. In Table 2 of Ref. (50) is found the amino acid analyses galactosamine. of the Tween 20 supematant and the Tween 20 residue. 6JGlucosamine, 11 &g, gaiactosamine, 4 ppig. ” Kagi (53) reports that histidine and aromatic amino acids are absent. +XNine residues of hydroxyproline, 76 &g/g of glucosamine, 55 CLglg of 4* Also found were 10.9 residues of cysteic acid, and 4.7 residues of galactosamine. omithine. 67 Glucosamine, 164 &g, galactosamine, 5 &g. 4sThe following are reported as moles/l00 moles of carbohydrate: BsThree residues of hydroxylysine, 3 j&g of glucosamine, 1 &g of N-acetylneuraminic acid, 9.0; galactose, 27.6; fucose, 21.7; N-acetylgalactosamine, 22.8; N-acetylglucosamine, 18.8; uranic acid, 0: sulfate, galactosamine. 69 Hydroxylysine, 0.5 residue, 113 pg/g of glucosamine, 6 LLg/B of 12.8. SoAlso found were carbohydrates (PmoYmg): galactose, 1.19; hex- galactosamine. ‘O Glucosamine, 1 I.Lg/g. osamine, 2.17; fucose, 0.52; sialic acid, 0.02. 7* Glucosamine, 34 &g. 51 Also found were carbohydrates @mol/mg): galactose, 1.44; hex‘* Glucosamine, 16 &g, galactosamine, 5 cLp/g. osamine, 1.66; fucose, 0.82: sialic acid, 0.02. 62The amino acid analysis of a minor component is given in Table I ra Glucosamine, 5 cLg/g, galactosamine, 27 kg/g. r4 Glucosamine, 1 &g. of Ref. (67). 75Two residues of hydroxylysine, 16 @g/g of glucosamine, 3 &g of s3 Glucosamine, 0. galactosamine. 54Glucosamine, 27 mol%. 76Glucosamine, 3 &g, galacto~mine, 2 &g. sj Glucosamine, 7’mol%. 77Glucosamine, 4 pdg, galactosamine, 1 pg/g. 56Glucosamine, 50 mol%. ?BFive residues of hydroxylysine, 29,329 pg/g of glucosamine. 5’ Glucosamine, 6 mol%. 74 Two residues of dihydroxyphenylalanine, 0.4 residue of hydroxyly58 Also in Table 2 of Ref. (73a) are the amino acid analyses of the acid-extract and acid-insoluble material. Phosphoamino acids expressed as sine, 765 cLg/g of glucosamine, 102 @g/g of galactosamine. 8o One residue of dihydroxyphenylalanine, one residue of hydroxyly3.5 mol% serine. See also Ref. (73b) for amino acid analyses of sine, 420 pgis of glucosamine, 11 &g of galactosamine. fractions of Walker tumor extracts. 81 Glucosamine, 23 p&g, galactosamine, 8 &g. 5y Also found were 3 residues of hydroxylysine, 80 mg/g of glucosamine, ** Glucosamine, 89 pg/g. galactosamine, 49 I*glg. and 265 mg/g of galactosamine. 83 Glucosamine, 8 &g. B” Also found were 16 residues of hydroxylysine, 245.7 mg/g of *4 Glucosamine, 962 &g, galactosamine, 25,156 p&/g. glucosamine, and 3 mgig of galactosamine. 85 Glucosamine, 0.2 &g. ‘* Also found were 0.4 residues of hydroxylysine, 644 mg/g of 86 One residue of hydroxylysine, 0.7 @g/g of glucosamine, 0.3 &g/g of glucosamine, and 248 mg/g of galactosamine. galactosamine. ‘* Also found were 5.7 mg/g of glucosamine and 57 mg/g of galactosamine. 87 One residue of hydroxylysine, 8 CLgig of glucosamine, 4 &g of 63 Also found were 12 residues of hydroxylysine. 10.0 mgig of galactosamine. glucosamine and 12 mg/g of galactosamine. $ \o
:
32
% s
iz
E ~
b ‘3 9
0
*@Seven residues of hydroxylysine, 8 I LLglg of glucosamine, 72 cLg/g of galactosamine. ss Glucosamine, 5 j&g. so Thirty-eight residues of hydroxyproline, four residues of hydroxylysine, 46 &g of glucosamine, 6 j~g/g of galactosamine. s* Glucosamine, 2 &g. 82Glucosamine, 0.7 beg/g, galactosamine, 0.8 @g/g. W Glu~osamjne, 30 F&g, galactosamine, 5 @g/g. w Nine residues of di~yd~xyp~enyla~ine, 186 pg/g of glucosamine, 64 ~~g/g of galactosamine. s5Glucosamine, 0.7 @g/g, gala~to~mine, 0.2 LLg/g. 96 Glucosamine, 1.5@g/g, galactosamine, 2 @g/g. 97 Glucosamine, 7 &g, gafactosamine, 1 w&g. sa Glucosamine, 8 &g. galactosamine, 9 &g. 99Glucosamine, 0.3 &g. r* One residue of hydroxylysine, 4 ccglg of glucosamine, 4 @/g of galactosamine. w One residue of hydroxylysine, 4 &g of glucosamine, 3 /&g of galactosamine. lo2 Glucosamine, 11 p&g, galactosamine, 4 &g. rW Glucosamine, 14 &g, gaiactosamine, 14 p&g. lw Seven residues of hydroxylysine, 64 &g of glucosamine, 88 &g of galactosamine. *05Glucosamine, 4 @g/g, galactosamine, 1 ,r&g. lo6 Hydroxylysine, 0.3 residue, glucosamine, 11 @g/g, galactosamine, 2 ccglg. rM Glu~o~~ne, 14 &g/g, galactosamine, 1.5tlgfg. ro8One residue of hydroxylysine, 20 &g of glucosamine, 2 &g of gatactosamine. ‘09 One residue of hydroxylysine, 232 y&g of giucosamine, 21 lLglg of galactosamine. If@Seven residues of hydroxylysine, 11 Leg/g of glucosamine, 11 pg/‘g of galactosamine. rrl Glucosamine, 37 pg/g.
rr2 Glucosamine, 15 ELg/g, galactosamine, 24 &g. ‘la Glucosam~ne, 41 &g/g, galactosamine, 30 LLglg. rl* Glucosamine, 4 &g, galactosamine, 5 I.L$l&. *I5 Glucosamine, 7 @g/g, galactosamine, 9 &g. rr8 Glucosamine, 4 &g/g, gaiactosamine, 5 .ug/g. r*t Glucosamine, 20 &g, galactosamine, 25 &g. rr8 Glucosamine, 14 &g, galactosamine, 16 &g. rln Glucosamine, 25 pg/g, galactosamine, 30 LLg/g. r20 Glucosamine, 5 g&g, galactosamine, 11 f.&g. r2r One residue of dihydroxyphenylalanine, 25 pg/g of glucosamine, 16 &g/g of galactosamine. r2* Five residues of dihydroxyphenylal~ine, 75 &g of glucosamine, 47 &g/g of galactosamine. 123Two residues of dihydroxyphenylalanine, two residues of hydroxylysine, 89 &g glucosamine, 19 &g galactosamine. rz4 Hydroxylysine, 0.7 residue, glucosamine, 22 @g/g, galactosamine, 4 lack. rz5 Glucosamine, 10 @g/g. I20 Hydroxylysine, 0.6 residue, glucosamine, 73 &g, galactosamine, 1.5E”g/g. rz7 Glucosamine, 139 @gig, galactosamine, 12 j&g. I*8 Glucosamine, 215 clg/g, galactosamine, 14 &g. lx* Glucosamine, 12 ItpJg. r30 Glucosamine, 15 &g, galactosamine, 4 @g/g. r3r Galactosamine, 79 &g. Ia2 Galactosamine, 53 &/g. *33Glucosamine, 28 &g, galactosamine, 16 EL&/g. 134Glucosamine, 6 pg/g. 135Glucosamine, 5 LLg/g. r3* Three residues of hydroxylysine, 5 &g of gIucosamine, 13 &g of galactosamine. r5’ Three residues of hydroxyfysine, 5 LLg/g of glucosamine, 14 &g of galactosamine. .. _^^ __. .. “.. lJs Nineteen resulues ot hydroxyproime.
Ia9 One residue of dihydroxyphenylalanine. WI Twelve residues of hydroxyproline. I41 Nine residues of dihydroxyphenylalanine. r4* One residue of hydroxylysine. I43 Two residues of dihydroxyphenylalanine. *U Five residues of hydroxylysine. 145Seven residues of dihydroxyphenylalanine. Ia6Twelve residues of hydroxylysi~e. 14r Four residues of hydroxylysine. I** Sixty-five residues of hydroxyproline. rl@Carbohydrate (%, w/w): glucosamine, 13; galactosamine, I50 Carbohydrate (%, w/w): glucosamine, 1.9; galactosamine, I51Carbohydrate (%, w/w): ghtcosamine, 3.2: galactosamine, lose, 12.3; sialic acid, 4.6. Is2Carbohydrate (%, w/w): glucosamine, 5.6: galactosamine, 1.6.
4.6. 0.4. 0.8; man-
IS3Residues of cysteic acid listed: 36.3. 154Carbohydrates (nmoUmg): D-&CO%, 134; o-gaiactose, 780; N-acetylo-galactosamine, 310; IV-acetyl-o-glucosamine, 286; mannose, 36: fucose, 26; glucuronic acid, 124. Is5 Half-cystine residues, less than 4: tyrosine, less than 1 residue: 17 residues of hydroxylysine; 99 residues of hydroxyproline. 156Half-cystine residues, hydroxylysine, hydroxyproline, and tyrosine: ail less than 1 residue. 157No residues of hydroxylysine or hydroxyproline detected. Is8 Multiply values for No. 11 by I. 1.5. Is9 Multiply values for No. 12 by 1.38. rW Multiply values for No. 13 by 1.15. I61 Multiply values for No. 14 by 1.25. IS2Multiply values for No. 15 by 1.53. lfi3 Multiply values for No. 16 by 1.17.
e z s E z
is !z
5 $
b Ei