ANALYTICAL

BIOCHEMISTRY

A Compilation

66,

303-329

(197%

of Amino

Acid

Residues DONALD

M.

Analyses

of Proteins.

VIII

per Mole-6 KIRSCHENBAUM

Department OfBiochemistry, Downstate Medical Center-SUNY.

Brooklyn. New York 11203

Received October 18. 1974; accepted December 30, 1974

This paper, as the others in this series (l-4) has been prepared following certain rules-(a) all molecular weights were rounded off to the nearest hundred for weights under 10,000 and to the nearest thousand for weights over 10,000, (b) the number of residues was rounded off to an integral number. Cysteine and cystine may have been determined as S-carboxymethyl cysteine or cysteic acid, the final results have been reported as residues of half-cystine. Similarly, methionine which may have been determined as its oxidation products has been reported as residues of methionine. Other analytical data have been reported as described in (1) and (3). Table 1 is the protein index listing 237 proteins and their sources. In addition, for some of the enzymes the Enzyme Commission number (EC) is given. Table 2 gives the amino acid analyses of the hydrolyzates of some of the proteins or of the sequences of other proteins. If the sequence is the source of the data it is so indicated with footnotes as is the amide distribution as asparagine and glutamine residues. In addition, if the carbohydrate content was also determined, this too may be found in the footnotes. Each protein listed in Table 2 has a citation to the original reference and for some of those proteins for which sequence data was used a citation to amino acid analyses by column chromatography is given. Some of the data is based upon the assumption of an integral number of residues for one amino acid and all the integral numbers for the other residues are related to it. When this was done it was mentioned in the footnotes. REFERENCES FOR TEXT 1. 2. 3. 4.

Kirschenbaum, Kirschenbaum, Kirschenbaum, Kirschenbaum,

D. D. D. D.

Anal. B&hem. M. (1972) Anal. B&hem. M. (1973) Anal. Biochem. M. (1974) Anal. Biochem. M.

(1971)

303 Copyright All rights

@ 1975 by Academic Press, Inc. of reproduction in any form reserved.

44, 159-173. 49,248-266. 52,234-254. 61, 567-609.

304

DONALD

M. KIRSCHENBAUM TABLE PROTEIN

1. Name Source 2. Name Source 3. Name Source 4. Name Source 5. Name Source 6. Name Source 7. Name Source 8. Name Source 9 Name Source 10. Name Source 11. Name Source

12. Name Source 13. Name Source 14. Name Source 15. Name Source 16. Name Source 17. Name Source 18. Name Source 19. Name Source 20. Name Source 21. Name Source

D-Galactose dehydrogenase Pseudomonas saccharophila Galactose operon: galactose epimerase Escherichia coli Galactose operon: galactose kinase Escherichia coii Galactose operon: galactose transferase Escherichia coli Galactose oxidase Dactylium dendroides @Galactosidase Escherichia coli p-Galactosidase, pH 4 Escherichia coli @Galactosidase Bacillus megaterium Galactothermin Human milk Gastricsin Pig Gastricsin Human Gastrin Pig gastric antra o-Gliadin Wheat cu,-Gliadin Hard red winter wheat G,-Globulin Human serum azn-Globulin Human urine &-Globulin Rabbit serum y,-Globulin, 0.6 s Human plasma y,-Globulin, 2 s Human plasma Globulin, progesteronebinding Guinea pig (pregnant) serum Globulin, thyroxine-binding Human plasma

1 INDEX

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 33. Name Source 34. Name Source 35. Name Source 36. Name Source 37. Name Source 38. Name Source 39. Name Source 40. Name Source 41. Name Source 42. Name Source 43. Name

al-o2 Globulin, urate binding Human plasma Glucagon Rat Glucagon Beef or pig Glucagon Duck pancreas Glucagon Human pancreas Glucanase, endo, EC 3.2.1.4 Trichoderma viride Glucanase, exo, EC 3.2.1.21 Trichoderma viride Exo-p-D-(l-+3)-glucanase Basidiomycete sp. QM 806 Glucoamylase I Aspergillus niger Glucoamylase II A. niger Glucoamylase I, EC 3.2.1.3 A. niger Glucoamylase I, EC 3.2.1.3 A. niger GIucoamylase I A. niger Glucoamylase R Rhizopus delemar Glucokinase Bacillus stearothermophilus D-Glucose isomerizing enzyme B. coagulans Str. HN-68 Glucose oxidase EC 1.1.3.4 Aspergillus niger Glucose oxidase, EC 1.1.3.4 A. niger Glucose oxidase, EC 1.1.3.4 Penicillium amagasakiense Glucose-6-phosphate dehydrogenase, subunit Human erythrocytes Glucose-6-phosphate dehydrogenase, EC 1.1.1.49 Neurospora crassa Glucose-6-phosphate dehydrogenase (Table continued)

4

COMPILATION

OF

AMINO

TABLE Source

44. Name 45. 46. 47.

Source Name Source Name Source Name Source

48. Name Source

49. Name 50. 51.

52. 53.

Source Name Source Name Source Name Source Name Source

54. Name 54a.

Source Name

55.

Source Name

56. 57.

Source Name Source Name Source

58. Name

59.

60. 60a.

Source Name Source Name Source Name Source

61. Name Source

ACID

62. Name

Aspergillus

63.

Source Name

a-Glucosidase Source 64. Name

A. fumigatus

/3-Glucosidase A. wentii

NADP-Glutamate drogenase Neurospora

dehy-

Clostridium

Source

65. Name

crassa

NAD+-glutamate dehydrogenase N. crassa Glutamate dehydrogenase N. crassa Glutamate dehydrogenase Rat liver Glutamate dehydrogenase Bovine liver Glutamate dehydrogenase Chicken liver Glutamate mutase, component S

Source

66. Name Source

67. Name Source

68. Name Source 69. Name Source

70. Name Source

71. Name

tetanomorphum

Glutamate synthase Escherichia

colt’

Glutaminase, phosphate independent Rat kidney Glutamine phosphoribosylpyrophosphate amidotransferase P-300 monomer Pigeon liver Glutamine synthetase Escherichia

coli

Source

72. Name Source 73. Name Source

74. Name

75.

Source Name

Glutamine synthetase Bacillus

subtilis

Glutamine synthetase, EC 6.3.1.2 Chicken retina Glutamine synthetase Rat liver Glutamine synthetase Rat brain Glutamine synthetase Pea Glutamine synthetase Sheep brain

VIII

305

1 (Continued)

Human erythrocytes a-Glucosidase fumigatus

ANALYSES.

Sowce 76. Name Source

77. Name Source

78. Name Source

79. Name

Glutaminyl-tRNA Escherichia

synthetase

coli

y-Glutamylcyclotransferase4.87 Pig liver y-Glutamylcyclotransferase4.95 Pig liver y-Glutamyltranspeptidase. EC 2.3.2.2 Rat hepatoma Glutamyl-tRNA synthetase Escherichia coli K12 Glutathione reductase Yeast Glutathione reductase Rice embryo Glutathione synthetase Human erythrocyte Glyceraldehyde-3-phosphate dehydrogenase Rabbit Glyceraldehyde-3-phosphate dehydrogenase Beef Glyceraldehyde-3-phosphate dehydrogenase Human Glyceraldehyde-3-phosphate dehydrogenase Chicken Glyceraldehyde 3-phosphate dehydrogenase Turkey Glyceraldehyde 3-phosphate dehydrogenase Pheasant Glyceraldehyde 3-phosphate dehydrogenase Halibut Glyceraldehyde 3-phosphate dehydrogenase Sturgeon Glyceraldehyde 3-phosphate dehydrogenase Lobster Glyceraldehyde 3-phosphate dehydrogenase (Table

continued)

306

DONALD

M.

TABLE Source

80. Name

Escherichia

8 1.

82.

Source Name

83.

Source Name Source Name

Bacillus

84.

Source Name

Bacillus

85.

Name

87.

Source Name

88.

Source Name Source

94. Name Source

E. coli

95. Name

96.

Source Name

97.

Source Name

98.

Source Name

99.

Source Name

cereus

Glyceraldehyde-3-phosphate dehydrogenase stearothermophilus

Glyceraldehyde-3-phosphate dehydrogenase Red kangaroo (Megaleia Glyceraldehyde-3-phosphate dehydrogenase Fish (Dissostichus mawsoni) Glyceraldehyde-3-phosphate dehydrogenase Honey bee (Apis mellifera) Glyceraldehyde-3-phosphate dehydrogenase Bumble bee (Bombus

Source

100.

Name Source

101. Name Source

102. Name Source

103. Name

nevadensis) 89.

Name Source

90.

Name Source

91. Name Source

Glyceraldehyde-3-phosphate dehydrogenase Bumble bee (B. appositus) Glyceraldehyde-3-phosphate dehydrogenase Bumble bee (B. occidentalis) Glyceraldehyde-3-phosphate dehydrogenase Bumble bee (Psithyrus suckleyi)

92.

Name Source

Glyceraldehyde-3-phosphate dehydrogenase Leaf-cutting bee (Megachile rofundata)

93.

Name Source

Glyceraldehyde-3-phosphate dehydrogenase Fleshfly (Sarcophage bullata)

Glyceraldehyde-3-phosphate dehydrogenase Screw-worm fly (Callitroga hominivorox)

Glyceraldehyde-3-phosphate dehydrogenase Yeast Glyceraldehyde-3-phosphate dehydrogenase Pig Glyceraldehyde-3-phosphate dehydrogenase

da) 86.

1 (Continued)

Glyceraldehyde-3-phosphate dehydrogenase

Source Name

Source

coli

KIRSCHENBAUM

Source

104. Name Source

105. Name Source

106. Name Source

107. Name

Source

108. Name Source

Glycerol-3-phosphate dehydrogenase Chicken liver Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Chicken liver Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Chicken breast muscle Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Chicken breast muscle Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Rabbit muscle Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Rabbit muscle Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Rabbit muscle Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Rabbit liver Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Rabbit adipose tissue Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Human liver Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Rat muscle Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Rat liver cytoplasm Glycerol-3-phosphate dehydrogenase, Fr. I, EC 1.1.1.8 Rat liver Glycerol-3-phosphate dehydrogenase, Fr. II, EC 1.1.1.8 Rat liver (Table

continued)

A COMPILATION

OF

AMINO

TABLE

109. Name Source 110. Solrrce Source 111. Name Source 112. Name Source 113. Name Source 114. Name Source 115. Name Source 116. Name Source 117. Name Source 118. Name Source 119. Name Source 120. Name Source 121. Name Source 122. Name Source 123. Name Source 124. Name Source 125. Name Source 126. Name Source 127. Name Source

Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Honey bee (Apis mellifpra) Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Bumble bee (Bombus nevadensis) Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Bumble bee (B. uppositus) Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Bumble bee (Psithyrus suckleyi) Glycerol-3-phosphate dehydrogenase, EC 1.1.1.8 Yellow jacket wasp (Vespula vulgaris) Glycerol kinase Escherichia coli Glycine N-methyltransferase Rabbit liver Glycinin Soybean flakes, defatted Glycogen synthetase Pig kidney Glycolic acid oxidase Pig liver Glycopeptide Penicillium charlesii Glycoprotein Human erythrocyte membrane a,-Glycoprotein, acid Human plasma Glycoprotein Bovine erythrocyte membrane Glycoprotein Pig aorta, intimal Glycoprotein B Beef aorta a,-Glycoprotein. acid Chimpanzee serum a,-Glycoprotein Rat serum a,-Glycoprotein Rat Yoshida ascites fluid

ACID

ANALYSES.

VIII

307

1 (Continued) 128. Name Source 129. Name Source 130. Name Source 131. Name Source 132. Name Source 133. Name Source 134. Name Source 135. Name Source 136. Name Source 137. Name Source 138. Name Source 139. Name Source 140. Name Source 141. Nome Source 142. Name Source 143. Name Source 144. Name Source 145. Name Source 146. Name Source 147. Name Source 148. Name Source 149. Name Source

q-Glycoprotein, acid Human serum u,-Glycoprotein, acid Human serum a,-Glycoprotein, easily precipitated Human serum a,-Glycoprotein Human serum cu,-HS-Glycoprotein Human serum a,-Glycoprotein, histidine rich Human serum cy,-Glycoprotein, Ba Human serum q-p,-Glycoprotein, 4s Human plasma PI-Glycoprotein Human plasma &,-Glycoprotein Human serum M- 1 Glycoprotein Bovine plasma M-l Glycoprotein Pig plasma M-l Glycoprotein Avian plasma M-2 Glycoprotein Bovine plasma M-2 Glycoprotein Pig plasma Glycyl-tRNA synthetase Escherichia coli Glyoxylic acid reductase. R, 0.22 isozyme Spinach Glyoxylic acid reductase, R, 0.19 isozyme Spinach Glyoxylic acid reductase, R, 0.17 isozyme Spinach Glyoxylic acid reductase, degraded form Spinach Halidohydrolase Pseudomonas dehalogenans Haptoglobin Human serum (Table continued)

308

DONALD

M. KIRSCHENBAUM

TABLE 150. 151.

152. 153.

154. 155. 156. 157.

158. 159.

160. 161.

Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source

162.

Name Source

163.

Name Source Name Source Name Source Name Source Name Source Name

164. 165. 166. 167. 168.

Source 169.

Name

170.

Source Name Source

1 (Continaed)

Haptoglobin, a’* chain Human serum Haptoglobin, ols chain Human serum Haptoglobin, (Y*,~ chains Human serum Haptoglobin, p chain Human plasma or ascites fluid Haptoglobin, p1-1 chain Human plasma Haptoglobin, p2-* chain Human plasma Haptoglobin, pz-r chain Human plasma Haptoglobin, PI-l chain Human plasma Haptoglobin & Human plasma Haptoglobin @2--Z Human plasma Haptoglobin P1-iML Human plasma Haptoglobin pz--IMb Human plasma Haptoglobin Pig plasma Haptoglobin, H chain Pig plasma Haptoglobin, L chain Pig plasma Helicorubin

172.

Helix

186.

pomatia

Hemagglutinin Vlex

173.

europeus

175. 176. 177. 178. 179.

180.

181.

Source

Hemagglutinin, compound III Lima bean (P. lunafus)

Name Source Name Source Name Source Name Source Name Source Name Source Name Source

Hemagglutinin-A

Name Source

Sophra

japonica

Hemagglutinin subunit Oyster (Crassostrea

Lens

culinaris

Hemagglutinin-B L. culinaris

Hemagglutinin L. culinaris, seeds Hemerythrin Worm (Golfingia gouldii) Hemerythrin A Worm (G. gouldii) Hemerythrin B Worm (G. gouldii) Hemerythrin Worm (Dendrostomum pyroides, coelomic) Hemerythrin Worm (0. pyroides, coelomic)

182. Name

Source Name

Hemerythrin Worm (0. pyroides, vascular) Myohemerythrin Worm (0. pyroides, Hemerythrin A

Source

Lingula

Name Source Name Source Name Source Name Source Name Source Name Source Name Source

Hemerythrin

Source

183. Name 184. 185.

187. 188.

189. 190. 191.

muscle)

unguis

B

L. unguis

Hemocyanin Mollusc (Octopus vutgaris) Hemocyanin Mollusc (0. macropus) Hemocyanin Mollusc (Eledone moschara) Hemocyanin Mollusc (Murex brandaris) Hemocyanin Mollusc

(M.

frunculus)

Hemocyanin Crustacea (Eledone spinifrons)

192. Name

lunatus)

171. Name

Hemagglutinin

virginica) 174.

II

Hemagglutinin, iso-phytoPea (Pisum sarirum) Hemagglutinin, iso-phyto-, heavy subunit Pea (P. safirum) Hemagglutinin, iso-phyto-, light subunit Pea (P. satirum) Hemagglutinin, compound II Lima bean (Phaseolus

Name Source Name Source

Source

Hemocyanin Crustacea (Homaris

Name

Hemocyanin

vulgaris) 193.

(Table

continued)

A

COMPILATION

OF

AMINO

TABLE

Soltrce

Crustacea (Palinurus

ACID

Source

195. Nume Source

214. Name Soitrce

Hemocyanin Crustacea (Callinectes

215. Name

supidus)

216. Nume

Hemocyanin Xiphosura (Limzzlus

217. Name

Sozzrce Source

polyphemus)

196. Name Source

197. Name 198. 199. 200.

Source Nume Source Name Source Name Sozcrce

201. Name Sozzrce

Hemocyanin Cancer

218.

magister

Hemocyanin Dolabella

219.

auricularia

cr-Hemocyanin Helix

220.

pomatia

/3-Hemocyanin

221.

H. pomatia

Hemocyanin Gastropod (Strophocheilzzs

222.

terrestris)

223.

Hemocyanin Gastropod (Pila Leopold

224.

Sozrrce Name Sol4rc.e Name Source Name Source Name Source Name Source Name Source Name

villensis)

202. Nanze Sozzrce

Hemocyanin Gastropod (Cymbiz4m

Sozrrce

204. Nume Source

205. Name 206. 207. 208.

Solzrce Name Sozzrce Name Soztrce Name Source

8-Hemolysin Staphylococcus

contortrix

209. Name Sozrrce

210. Name 211. 212. 213.

Source Nczme Source Name Source Name Source

Histidine ammonia-lyase Pseudomonas ATCC 1 I299b Histidine decarboxylase Micrococcus sp. n Histidine decarboxylase Luctobncillus 30a Histidinol dehydrogenase Salmonella

typhimzrrium

Histidinol-P aminotransferase. EC 2.6.1.9 S. typhimurium

Histidyl-tRNA

226.

Escherichia

227.

Source Name Soztrce

228. Name Source

229. Nume Sozzrce

230. Name Sozrrce

231. Name

laticinctus)

Hepatocuprein Human liver Hexokinase, P-i Yeast Hexokinase, P-II Yeast Hexokinase L, Wheat germ Hexokinase L,, Wheat germ

Pseudomonas

Name Soltrce Nume

aureus.

mutant of Wood 46 strain &Hemolysin S. aureus strain Foggie Hemopexin Human serum Hemopexin Human serum Hemopexin Rabbit serum Hemorrhagic principle Broad banded copperhead venom (Agkistrodon

Hexokinase Rat brain Hexokinase Bovine brain Hexokinase Pig heart Hexose oxidase Alga (Chondrzzs crispus) Hirudin Leech (Hirudo medicinulis) Histidine ammonia-lyase

Source

225.

neptuni)

203. Name

309

VIII

1 (Continued)

vulgaris)

194. Name

ANALYSES.

232.

Soztrce Nome Soizrre

233. Name Sozrrce

234. Name 235.

Source Name

Swrcr

synthetase

S. typhimzzrizzm

Histidyl-tRNA

synthetase co/i

Hormone-binding polypeptide Pig posterior pituitary Hyaluronidase Tarantula venom (Dugesiella hent5 (Girard)) Hydrogenase Clostridium

pastezrriunzmz

Hydrogenase Desulfovibrio

vulgaris

3-Hydroxyacyl-CoA dehydrogenase Pig heart D(-)-P-Hydroxybutyrate dehydrogenase Beef heart P-Hydroxydecanoyl thioester dehydrase Escherichia

coli

Hydroxypyruvate Pseudomonas

reductase

acidovorans

17p-Hydroxysteroid dehydrogenase Human placenta

2

25 12

Reference

M, x 1O-3

1”

25 44 20 24 15 10 10 7 13 24 3 6 6 13 5 8 4 2 191

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia

Amino

40

33 39 36 30 22 14 14 12 37 51 10 10 16 13 7 13 9 2 _

2

40 2

33 29 31 30 19 23 20 16 46 32 4 9 15 13 10 10 14 6 -

3

6

135 5

55 85 34 93 18 75 19 110 13 48 23 67 33 67 28 65 42 123 29 142 619 8 24 21 29 22 74 8 36 14 45 5 36 35 -4 -115

5

40 47 34

20 38 24 31 8 24 14 21 39 42 -* 7 14 17 13 15 10 11 -3

4 8 59 66 54 78 32 42 6.5 49 100 113 1313 46 26 24 36 44 28 100 7

7 259 92 22 26 15 26 202 43 85 141 1 81 0 15 8 13 96 6 145 8

2 3 2 3 2 3 13

1 6 13 21 6 28 2 4 7 19

9

36 33 9

31 19 19 30 13 15 32 23 26 39 6 4 4 4 1 19 16

10 33 18 23 25 13 17 32 21 26 39 6 5 0 3 1 15 17 444 31 9

11

13 10

6 4 4 9 9 7 5 5 14 13 2= 3 7 2 6 4 8

12

per molecular

Residues

2 COMPOSITIONS

TABLE ACID

AMINO

5 5 9 16 9 26 10 3 6 72 4 2 1 4 4 7 6 2 64 50 11

13

weight

7 7 12 21 12 39 14 4 8 104 5 3 1 5 5 10 8 1 -’ 31 12

14 15 28 23 44 7 23 35 28 37 47 24 6 35 12 12 16 14 2 32 508 13

15

of protein

4 10 14 14 11 85 6 14

12 14 14 139 4 2 11 m 29 20 42

16

2 15

1 8 4” 4 5

3 2 10 7 3 -10 6 4 15 11

17 1 3 2 5 1 3 3 3 2 9 0 0 12 0 0 1 2 0 6 5.1’2 16

18

14 9 11 I1 4 5 10 11 14 11 413 0 10 5 2 4 5 2 19 14 17

19

35 22 25 35 14 17 27 23 42 36 7 24 13 10 19 13 9 14 14a 18

20

8 5 25 16 10 18 10 4 58 19

25 31 23 44 9 30 34 25 38 52

21

59 32 23 25 11 21 64 24 34 62 -14 6 15 12 22 13 12 30 57 20

22

”

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia M, x 1O-3 Reference

Amino

24

25

1 1 1 111 111 222 000 000 444 334 443 333 000 1 1 1 111 222 111 222 222 -11 4 315 - 21 22 23

23”

24

1 1 1 2 0 0 4 3 4 3 0 1 1 2 1 2 2 1 416

26

2 12 15 9 18 17’” 93 49 25

62 46 30 36 30 21 40 44 74 46 -17

27 55 50 25 32 21 35 46 38 65 35 3 5 14 16 7 19 1816 130 77 25

28 49 36 28 19 22 18 49 35 45 26 4 3 7 10 6 12 18 14 71 51 26

29 59 78 46 53 27 29 119 104 83 56 8 4 16 23 6 27 30 30 2119 99 27

30 63 82 46 56 25 29 121 103 85 45 8 4 16 22 6 28 29 32 5320 112 27 -

31

Residues

47 64 38 46 22 23 77 72 69 45 77 12 13 18 44 22 26 19 -62 28

32

62 28

21 27 -

13 18

47 66 38 45 21 22 81 75 73 47

33 66 90 55 61 32 33 132 119 93 65 8 4 19 25 6 32 34 33 110 29

34

per molecular

77 87 58 57 36 31 108 88 104 48 6 6 39 18 8 34 44 36 -21 27

35

weight

35 30

90 88 60 60 40 22 22 44 48 60 8 14 14 30 28 14 12 6 -

36

37 106 140 53 134 51 44 70 87 182 136 0 27 120 61 49 96 58 13 80 160 31

of protein

111 108 79 96 46 53 85 82 130 99 4 21 30 45 37 35 52 22 159 1502* 32

38 117 127 84 105 54 49 64 84 145 111 7 21 33 46 32 35 53 21 150 152 33

39 111 124 91 116 55 44 63 74 157 120 7 30 60 35 18 54 39 25 220 150 33

40 26 22 21 33 17 21 19 16 38 43 7 9 19 22 9 18 13 5 40 34

41

continued)

(Table

48 -24 37

38 43 26 30 14 17 54 48 51 32 4 2 9 10 3 15 17

164 132 126 193 93 144 114 94 227 260 40 52 117 108 54 105 80 30 240 36

111 96 93 140 103 83 108 79 185 183 58 62 131 105 39 74 72 25 -23 200 35

44

43

42

z

34 20 16 20 14 7 27 23 37 21 3 3 10 4 6 12 15 -25

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia M, x 10-S Reference

52 41 38

45O

acid

Amino

132 111 78 94 46 70 76 67 159 124 8 14 38 53 11 36 59 21 71z6 168 39

46

36 35 22 24 12 10 23 13 25 36 4 5 19 112’ 6 12 10 5 28 34 40

47

29 32 27 42 26 20 33 22 51 47 4** 9 29 27 11 22 18 1 49 52 41

48 56 54 35 40 17 15 29 14 41 55 6 9 30 16 9 16 15 7 49 42

49 38 28 26 26 28 19 23 21 39 33 10 26 22 12 15 14 4 50 43

50 47 37 34 31 37 21 30 28 50 45 6 13 33 30 14 23 18 330 34*9 55 44

51 48 40 33 32 35 20 28 27 48 48 7 15 35 28 16 23 17 3 -31 56 48

17 11 14 10 12 5 8 8 18 16 5 4 12 3 3 6 3 1 17 17 49

53

50

149 149 109 142 76 71 70 74 165 157 18 36 75 97 30 58 42 18 -32

54 70 78 70 61 47 44 61 53 74 76 7 17 41 40 17 32 29 9 98 993= 50a

54a

per molecular

Residues 52

2 (Continued)

TABLE

40 41 33 49 20 24 25 24 41 34 18 9 28 25 10 14 13 -33 50 51

55

weight

37 44 30 33 26 25 28 39 46 40 4 16 26 19 26 23 16 4-53 5334 52

56 35 24 19 20 15 20 24 17 35 31 18 24 19 20 14 4236 55

5035 54

58

26 40 26 37 26 29 20 20 44 51 4 12 29 23 12 29 16

57

of protein

42 28 20 25 23 23 24 20 48 33 12 12 25 21 13 21 17 64536 56

59

4536 56

41 28 18 25 22 29 21 20 47 41 13 26 23 13 23 16

60 26 29 27 40 23 19 26 23 42 41 2 6 26 19 8 28 14 6 45 56a

60a

57

50037

463 322 196 247 233 270 269 222 461 486 120 119 272 276 122 225 177 76 -

61

63 35 16 40 12 35 11 41 15 32 11 29 9 25 13 25 9 59 19 57 32 18 3 13 4 31 17 34 7 15 3 22 8 20 8 2 --69 22 58 59

62

22 59

15 12 12 16 11 10 14 9 18 31 4 4 17 7 3 8 7 2

64

”w

65”

37 39 40 52 26 35 39 44 54 70 4 8 32 24 II 29 13 17 -38 113 60

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia M, x 10-S Reference

Amino

81 90 57 58 50 29 51 46 100 92 8 19 78 54 42 24 23 8 102 61

66

49 38 53 41 33 16 2 8 60 58 5 12 24 9 9 20 9 48 4839 62

67

51 39 39 35 29 23’O 44 31 47 46 7 5 30 20 8 20 13 51 52io 63

68

116 135 98 152 61 59 109 64 112 160 42 33 73 72 27 53 30 150 64

69 113 114 105 62 66 43 58 70 1314’ 71’” _ 31 90 34 34 48 30 12 -42 120 65

70 112 111 110 64 63 43 57 71 131”’ 74”’ 30 90 35 34 48 31 13 120 65

71 117 108 95 65 65 42 68 70 l391’ 7411 31 84 31 31 46 31 13 120 65

72 115 121 116 64 58 42 61 68 13841 644’ 30 84 34 30 44 31 12 120 65

73

Residues

115 120 117 65 58 42 62 68 1374’ 634’ 31 87 35 31 45 31 13 120 65

74 112 117 110 67 56 42 59 66 134” 6241 _ 31 84 36 32 46 31 13 120 65

75

per molecular

94 106 105 61 71 41 72 59 11041 77”’ 28 87 35 42 50 32 13 120 65

76

weight

197 111 118 64 67 42 58 68 1304’ 654’ _ 29 97 37 20 46 39 12 120 65

77 30 32 38 18 18 12 25 20 32 24 5 10 28 9 5 15 9 3 174” 363fi 67

7g

of protein 80

81

106 124 26 124 140 32 105 127 37 69 81 21 58 66 19 31 36 12 50 56 29 92 112 23 14ES4’ 181 36 76” 89 19 _ 16 2 24 33 6 87 105 26 36 49 11 19 24 8 37 45 10 28 3311 28 16 3 140 -44 120 144 36”” 65 68 69

79 32 32 34 18 21 12 19 22 38 18 4 9 26 10 11 14 9 3 17dj 36”6 71

82

(Tddc

30 -47

32 23 32 36 38 31 32 41 35 21 27 19 21 20 21 10 11 11 14 18 18 24 18 22 40 37 36 27 28 20 224 787 25 22 28 13 15 11 7 910 12 5 14 7 8 10 ----144 -46 72 73 74

cwrlti~lwd)

10 4 36 75

39 20 4 9 28 11 11 -47

-47

17 19 -47 -47

-47

86

84

85

83

E

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammoni M, x 10-S Reference

Amino

a

30 37 32 20 24 11 19 18 36 23 5 5 30 9 666 12 12 ----------36 76

87”

36 76

12 11

12 11

36 76

31 38 33 20 25 14 19 17 38 20 3 5 26 11

89

30 36 32 21 26 15 21 16 38 20 3 5 26 11

88

36 76

30 38 34 20 25 14 20 16 38 20 3 5 26 11 666 12 11

90

36 76

12 11

30 37 31 21 25 14 21 16 38 21 3 5 27 11

91

36 76

13 11

31 34 30 20 27 14 23 16 40 19 3 5 26 11

92

36 76

30 37 36 19 20 13 24 22 40 16 3 5 26 10 554 14 9 -_ ---

93

36 76

13 5

16 8

30 77

2

26 19 24 21 24 12 13 13 24 31 9 6 20 12

95

30 35 37 19 21 14 25 23 38 17 3 4 25 10

94 97

98

per molecular

2 (Continued)

35 78

30 77

35 78

29 30 34 21 22 24 27 25 28 23 23 26 26 22 23 14 13 15 14 11 12 14 14 15 2748 24 2748 41 33 37 10 10 11 6 8 9 23 20 22 13 6 7 5 67 15 11 12 5 4 5 2222-43232282 _ __

96

Residues

TABLE

41 38 79

40 34 32 30 27 16 12 13 2849 41 10 8 30 8 9 15 4

99

weight

--------78 80

89 63 58 64 59 41 21 21 47 94 16 59 16 21 31 9

100

75 81

80 64 54 56 52 32 28 28 56 84 20 18 56 16 18 30 8

101

of protein

77 81

71 61 57 65 46 34 34 30 62 84 11 52 25 17 29 12

102

38 82

37 31 31 29 26 16 10 14 2748 41 10 9 28 9 9 15 4

103

70 80

66 54 48 65 46 35 30 27 51 81 13 52 25 17 29 12

104

29 83

26 22 25 25 21 12 14 14 23 26 9 2 20 8 7 12 3

105

30 84

29 22 23 26 18 12 15 13 23 33 7 5 19 8 7 12 4

106

29 85

28 21 19 26 16 14 11 11 2150 28 6 4 24 12 10 11 5

107

29 85

31 24 22 24 18 12 17 14 2251 33 4 18 7 8 10 3

108

g

--

37 86

28 26 32 29 26 11 11 20 34 34 11 6 24 16 6 12 6

-

29 26 32 29 24 11 11 19 33 35 11 6 24 16 7 12 7

24 29 29 30 30 11 10 22 35 34 11 3 22 17 6 13 6 -52 37 86

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia M, x 10-Z Reference

111

37 86

110

109”

acid

Amino

37 86

28 26 33 30 25 10 9 20 34 36 11 6 25 15 6 12 6

112

37 86

-

25 27 27 28 26 14 13 16 33 36 9 5 29 15 6 13 4

113 41 44 35 35 33 14 21 34 46 59 5 15 22 30 8 14 17 11 40 -= 88

114 93 86 75 85 22 27 61 54 86 88 16 16 48 44 45 32 39 18 -54 124 89

115 230 158 148 216 130 210 204 120 364 612 44 30 136 178 58 118 86 23 _ 350 90

116 248 240 166 339 130 130 234 160 325 495 48 60 236 204 73 125 92 0 370 91

117

Residues

33 44 42 47 23 18 24 21 43 46 7 12 33 30 5 13 13 7 -55 92

118 3 4 2 -56 -56 2 9 6 1 1 -56 tr2 1 tr* tr2 tr2 27 93

119 13 11 17 13 14 15 28 22 12 20 4 8 9 8 3 6 94

120

per molecular

10 13 -5’ -57 10 11 10 18 24 -57 6 -57 17 9 4 11 12 4 -57 44 95

121

weight

36 41 31 40 25 35 63 43 35 56 12 8 18 27 30 16 21 180 96

122 31 39 34 24 74 35 23 27 59 81 35 3 48 22 14 27 23 5 -56 71 97

123

of protein

8 10 9 15 8 9 8 17 -60 -60 -60

125

-60 11 -60 -6D -60 -60 -59 -60 6.4 39 98 99

3 3 2 4 1 2 3 3 5 4 0 02 2 1 1 2 1

124 13 20 10 30 10 14 13 28 39 42 10 5 28 15 7 22 26 -61 45 100

126 14 17 15 38 14 12 11 23 34 44 4 5 26 14 6 27 20 _ -61 45 100

127

(Table

13 -62 44 101

9 11 10 18 11 9 9 19 26 37 4 2 17 11 4

128

24 26 26 40 12 23 23 23 33 45 0 5 21 15 11 17 8 4 4564 50 103

130

continued)

102

5 6 6 9 6 5 3 9 12 34 2 5 5 2 6 6 -63 -

129

w o\

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia M, x 10-Z Reference

Amino

8 9 10 15 10 8 7 18 22 36 3 1 15 10 4 10 11 3 465 44 103

131”

23 38 35 30 8 41 20 20 32 42 11 1 16 11 12 10 7 2 4366 49 103

132

28 16 19 27 12 49 25 12 51 45 15 0 16 27 47 24 12 2 4167 59 104

133 19 25 30 32 20 29 21 28 46 46 12 3 23 9 5 16 14 8 4868 60 106

49 105

135

21 36 33 28 6 39 18 19 30 40 7 1 16 7 11 12 6 3 _

134

31 107

9 10 9 15 9 8 8 15 21 30 5 1 14 8 3 10 9 3 1269

136

40 103

18 14 15 15 10 27 18 22 23 22 18 3 24 8 4 14 12 4 2810

137

42 108

13 19 17 49 17 14 15 17 32 36 2 19 11 8 18 8 -71 47 108

11 16 8 19 14 11 9 10 27 32 6 2 22 7 9 9 8 -72

139

44 108

11 21 14 19 7 13 11 16 19 33 4 4 11 9 12 11 3 -73

140

5.5 108

13 21 13 18 18 11 13 9 25 41 7 3 25 12 6 16 12 -74

141

per molecular

Residues 138

2 (Continued)

TABLE

54 108

15 27 28 45 17 22 16 20 36 33 4 22 15 9 21 8 -76

142

weight

22.5 109

138 220 134 222 79 108 75 105 220 259 ST6 36 112 123 31 92 57 22 _

143

145

98 110

98 110

67 78 85 83 62 61 71 72 40 41 38 36 4748474711 41 41 73 72 77 72 12 12 24 24 49 49 33 33 11 11 24 24 21 20 12 10 _ _

144

of protein

83 110

37 63 63 8 20 42 25 8 19 15 13 _

42 72 75 12 23 50 34 11 23 19 16 _ 98 110

73 67 52 57 36 32

147

69 84 60 70 39 37

146

15 111

7 11 16 1 2 7 6 5 4 2 0 -77

16 16 11 7 13 9

148

100 103

51 50 63 53 30 43 40 44 83 75 20 8 64 14 23 16 34 14 918

149

151

152 7 I 12 5 5 8 8 8 12 3 3 6 3 3 5 7 7 11 2 2 3 3 3 5 15 15 23 8 9 16 3 3 6 0 0 0 9 8 15 2 2 4 2 2 4 0 0 0 5 5 10 I 1 2 13’9 1379 20 -80 112 112 112

150

,” .J

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia M, x 10-a Reference

Amino

154

20 24 21 25 27 31 23 27 13 15 13 12 15 20 19 21 28 31 29 33 6 5 4 4 22 25 5 5 10 11 8 9 12 12 5_ -81 40 113 114

153”

24 23 29 27 13 15 18 21 33 33 5 5 26 7 11 9 11 -81 40 114 -~.___

155

24 25 31 27 16 15 16 20 33 33 5 5 26 5 11 8 10 -81 40 114

156 21 22 24 24 13 15 16 19 28 29 4 3 22 5 10 8 12 -82 40 115 .-

157 20 21 26 23 13 13 15 18 29 28 5 4 23 4 10 8 1’ -112 40 115

158 22 22 26 23 14 12 15 19 29 28 5 3 23 5 10 9 10 -82 40 115

159 19 20 22 25 12 13 16 18 29 33 4 4 21 6 9 10 10 -82 40 115

160 20 21 24 24 12 13 16 18 28 31 5 4 21 5 10 9 12 -82 40 115

161

Residues

54 50 66 66 34 40 36 58 92 78 18 12 76 18 22 14 2883 12 t 14 -83 116

162

165

weight

-83 118

1 64 24 20 60 35

38 49 54 47 39 39 66 57 1008” 64

166

of protein

26 7 20 19 5 12 22 8 6 28 3 5 14 1 2 14 7 13 16 2 7 22 8 10 40 10 14 28 II 8 ---R44 5 0 0 26 7 5 4 2 1 5 3 3 9 0 5 IO 5 2 -]_ 12 116 116 117

163164

per molecular

24 31 40 21 16 13 27 41 47 25 0 0 23 8 7 25 15 11 -86 55 119

167 7 9 10 6 5 4 6 13 18 8 0 trz 6 2 1 8 4 2 -HI 18 119

168

170

171

172

(Tub/e

3 14 14 80 4 16 16 95 16 15 86 6 4 20 20 88 1 9 9 60 8 42 1 9 7 19 18 116 4 11 11 89 2 23 22 98 4 12 12 80 02258 0 000 1 11 10 36 I 2 217 1 3 3 23 2 11 10 51 4 2 3 33 2 5 6 33 -RR 11 31 31 133 119 120 120 121

169

0 22 9 8 28 14 12 48 123

-91

30 33 45 19 18 19 40 53 57 34

174

continued)

122

-99

-89

2 0 7 17 4 3 2

14 12 5 12 6 6 6 10 27 15

173

g

32 33 45 19 18 18 44 56 53 33

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia M, x IO-3 Reference

0 26 10 10 28 15 12 48 123

-91

175a

acid

Ammo

63 124

-99

52 53 58 28 28 25 57 92 65 39 0 4 24 5 4 36 8 8

176

178

179

7 77667 5 56657 4 44334 8 8 8 9 89773 4 4 4 4 4334 4 4 4 17 19 17 10 10 9 l--l13 1 1 1 11 11 11 3 33435 7 76676 9 99767 5 55556 4--343 10 -93 126 126 125

177

1 9

14 129

13 128

5 18 11

9

181

1 9

6 18 11

4.-

10

180

2

15 128

5 9

494 17 13

294

6

10

182

594

6 7 7 7 5 6 494

183

130

15 1 4 8 4 6 9 3 -

1495

6 6 5 9 5 5 4 7

184

24 18 7 51 131

2296

22 28 26 38 22 24 21 22 49 40 10 11 20 16

186

weight

7 7 5 9 4 5 4 7 1495 1.5 1 4 9 4 6 9 3 -

185

131

per molecular

(Conrimed)

14 13 2 3 13 2 4 6 4 3 14 128

Residues

TABLE

51 131

25 28 24 40 24 23 23 26 49 43 8 10 21 199’ 24 24 19 6 -

187

of protein 189

24 26 27 28 24 24 37 37 22 17 22 22 23 20 21 22 50 51 40 48 9763 10 9 19 18 16 20 25 29 23 27 17 16 77 ---51 51 131 131

188

51 131

10 20 20 28 27 17 7

27 29 25 38 18 22 21 22 52 49

190

75 131

16 25 29 43 37 23 10

36 38 41 45 27 28 34 33 81 62

191 36 36 40 45 30 28 26 37 79 68 5 14 29 29 40 34 21 7 75 131

192

75 131

39 35 40 45 32 30 25 31 94 72 5 19 28 31 42 35 21 8 ----

193

75 131

43 45 44 48 32 31 30 33 88 72 6 16 30 31 38 36 26 8

194

75 131

36 30 41 52 33 26 30 31 71 70 10 15 36 31 46 32 22 -

195

78 133

40 38 48 49 30 32 36 36 95 68 3 16 32 31 41 39 29 12

196

_w \o

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Hi&dine Phenylalanine Tyrosine Tryptophan Amide ammonia M, x 10-z Reference

Amino

198

31 13 39 15 32 13 46 20 20 9 25 12 39 12 21 11 58 23 49 19 14 3 6 2 19 9 24 9 14 11 29 11 23 10 10 6 63 -sg 56 25l”” 134 135

197”

50 137

25100

125

-99

25 28 24 39 21 24 26 24 51 46 4 2 17 19 19 25 20 12 -101

200

12 13 12 17 9 11 9 10 24 20 3 2 9 9 11 12 11 5

199

50 137

26 33 26 38 19 27 25 22 48 50 5 5 14 23 18 24 17 13 -102

201

50 137

26 28 24 38 18 20 25 22 48 47 2 10 20 20 20 27 19 13 -102

202

5.1 139

-

3 2 3 2 7 0 2 4 6 2 0 2 7 0 0 2 0 1103

203

205

207

208

weight

49 42 4 33 26 3 28 26 2 41 37 4 10 11 2 37 29 8 32 32 3 25 24 3 46 45 8 45 38 5 12 10 9 4 4 1 26 23 9 23 23 2 20 17 3 22 19 2 16 14 2 2 18 18 55105 49106 8.2 141 141 142

206

per molecular

45 45 39 32 31 28 45 42 59 11 3 38 40 33 47 27 74 45 42 48 011 25 7 88 26 4 23 2 19 48 21 7 18 10 18 66 621°” 68 80 140 103

204

Residues 210

211

40 48 42 21 32 33 24 28 27 35 19 49 16 30 36 11 25 29 25 21 23 16 30 29 37 56 53 29 52 54 4 8 4 0 11 11 23 381°7 34’0” 8 18 18 13 8 5 8 18 23 0 15 15 -107 4 -34 50 50 143 144 144

209

of protein

50 97 89 tr2 30 59 55 18’09 37

80 48 65 83 49 35

214

48 48 146 146 148

---

46 45 43 34 36 36 39 40 22 21 19 26 282647 22 20 48 49 55 55 4 3 7 6 31 32 17 17 8 7 16 16 131120 ---

212213

147

-

149

-

9 1 3 4 2 3 4 4 10 13 6 0 -111 1 2 2 0

218

9.1 150 151

--

217

79 18 55 14 60 10 85 8 49 4 26 9 49 14 51 10 104 20 93 20 3 24 2 61 5 51 3 18’09 l”o 37 6 22 2 -

216

(Table continued)

78 48 57 87 42 21 51 51 90 96 tr* 30 57 45 18lo9 39 18 -

215

g

219”

144 255 143 187 79 75 101 57 128 157 17 37 32 87 48 34 19 6 210 152

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia M, x 1O-3 Reference

Amino

40 31 99 52 43 19 11 215 153

153 311 164 224 77 77 121 64 157 166 -113

220

45 11 75 110 154

28 67 30 9 -114

66 39 70 39 118 107 -114

76 63 45 -114

221 22 54 29 35 19 23 30 27 32 40 6 4 13 19 4 10 6 2 34 40 156

28 26 15 18 17 21 19 16 45 33 2 10 24 11 2 9 15 7 37 155

223

222 19 29 27 36 16 18 18 22 33 44 9 2 9 21 2 10 10 4 37 157

224 64 73 61 81 35 20 29 33 70 91 8 1.5 34 53 13 20 20 80 158

225 76 72 40 84 29 23 37 35 63 83 8 10 36 16 37 22 4 2 84 159

226

227

weight

14 7 2 7 2 6 7 2 5 13 12 1 2 5 0 3 1 0 8 9.2 160

per molecular

2 (Co&rued)

Residues

TABLE

31 18 17 20 16 22 28 22 36 32 13 4 48 9 6 15 13 6 40 161

228

60 162

36 50 58 50 54 18 28 38 53 23 4 14 50 16 14 24 22 0 -115

229

of protein

45 163

46 44 32 32 23 24 13 19 40 41 6 12 31 15 8 15 12 4 _

230

67 164

41 57 48 59 23 26 52 48 54 54 2 14 66 15 14 30 12 2 -

231

32 165

32 23 21 20 13 12 23 17 24 29 6 9 18 17 7 11 10 4 -

232

42 23 27 35 13 14 8 15 34 29 4 11 24 16 4 17 8 5 29 36 166

233

63 81 45 50 26 24 33 28 61 61 3 12 40 23 20 16 11 4 74 167

234

50 54 47 66 7 31 34 29 40 51 10 5 20 37 11 20 9 2 68 168

235

c

LLProtein number corresponds to that given in Table 1. 1 Determined as ammonia released after hydrolysis of the protein with I N HCl for 10 hr at 105°C. 2 -, Not determined; tr, trace. 3 These values calculated from (3) assuming a molecular weight of 40,000. See footnote c in Table V of Ref. 2. 4 Single analysis without correction for decomposition of any amino acids. 5 Assumed seven residues of aspartic acid as basis of calculation. B The calculated residues per mole were obtained by assuming cystine equal to unity. 7 Amino acid analyses of cY-gliadin fractions given in Table II of (12). 8 There are also 7 residues of hexose, 5 of acetylhexosamine, and 1 of fucose; no acetylneurarninic acid found. 9 Analyses calculated on the basis of 13 residues of leucine per molecule. lo 7-8 residues of proline. ii Analyses calculated on the basis of 4 residues of arginine per molecule. i* Negligible amounts of hexose, hexosamine and sialic acid (16). r3 Spectrophotometric titration withp-hydroxymercuric benzoate did not reveal any sulfhydryl groups (17). I4 There are 5-6 residues of half-cystine and 43 residues of ornithine per molecular weight of 57,000 (65,000 less 12.1% carbohydrate). The values given include no correction for destruction or incomplete hydrolysis of amino acids. 14aCarbohydrate, moles per mole protein: mannose, 52; galactose, 34: N-acetylglucosamine, 61; N-acetylgalactosamine, 4; fucose, 4; sialic acid, 14. l5 From sequence. There are 3 glutamine residues present. The amino acid analysis is also given in (23). I6 From sequence. There are 3 glutamine and 1 asparagine residues present. The amino acid analysis is also given in (24). I7 O-l residue of half-cystine. *RIn Table III of Ref. (25), there is given for proteins 27 and 28: Thyroxine. 17 and 18 residues. I believe this is a misprint and should be tyrosine.

I9 69 residues mannose, 16 residues glucose, and 2 residues galactose. *O128 residues of mannose, 20 of glucose, and 3 of galactose. 2120 residues of 2-amino-2-deoxy-o-glucose (glucosamine). 22 Number of amino acid residues calculated on the basis of a molecular weight of 150,000 and on basis of 16% carbohydrate and 2 moles of FAD. 23 15.5 mole percent ammonia; one determination. 24The data reported are from a 24-hr hydrolysate. The results of a 72-hr hydrolysate are given in (37). Carbohydrate is present to the extent of 14%; as residues per mole of protein: glucosamine, 3.2; mannose, 55.1; glucose, 5.4. 25 As residues per mole of protein: glucosarnine, 1.84; mannose, 16.6; glucose, 32.5. 26Moles per molecular weight: glucosamine, 52; hexoses, 156. *r Based on 11 arginine-containing peptides. 28 Based on 4 cysteines per subunit. 29 Data from sequence; the amide ammonia is distributed as 21 asparagine residues and 13 glutamine residues. Amino acid analyses of hydrolysates can be found in Ref. (43, 45-47). 30 Recently an additional tryptophan residue was reported (44a) making a total of 4 residues per molecular weight. 31 From sequence. 32 M,is reported as 800,000 (50) but the amino acid analysis is for 200.000 g of protein. 32a56 residues of hexosamine. 33 In (51) the amino acid analyses of the P-300 dimer is also given. 31Assumed minimum molecular weight. See also Ref. (53). 35Assumed minimum molecular weight. 36Subunit molecular weight. 37These values are the average of the analyses of two preparations of the enzyme. The amino acid composition is reported for 500,000 g of protein. This is not the molecular weight of the protein. In Ref. (56) the amino acid composition has been recalculated for 45,000 g of enzyme, and in Ref. (55) the same thing has been done for 42.000 g of protein.

i

38 The following are given in residues per mole (113,000 g) of protein: hexose, 134; hexosamine, 30; fucose, 0; sialic acid, 33. 39Data reported per mole of FAD. Molecular weight including FAD is 48,800. *OData reported as moles of amino acid per mole of FAD. There is 1 mole of FAD per 52,000 g. Hydroxyproline was present in “appreciable amounts” (63). 41 The data for aspartic acid are reported in (65) as asparagine and for glutamic acid as glutamine. 42 Additional data on this protein from rabbit may be found in (66). *3 From sequence; the amide ammonia is distributed as 10 asparagine and 7 glutamine residues. There is an N-terminal acetyl group. Amino acid analyses may be found in (65) and (67). e From sequence; amino acid analyses may be found in (65). 45From sequence; the amide ammonia is distributed as 12 asparagine and 5 glutamine residues. Amino acid analyses may be found in (66) and (70). 46Number of residues have been calculated from the quantities recovered by amino acid analyses after normalization to 152 residues of the stable amino acids. 47Residues per 36,250 g: threonine, 21-22; serine, 19-20; proline, 13-14; alanine, 35-36; valine, 30-31; phenylalanine, 13-14. 48Data based on 27 residues of aspartic acid. 49Data based on 28 residues of aspattic acid. soData based on 21 residues of aspartic acid. 5* Data based on 22 residues of aspartic acid. s2See (87) for an earlier analysis that included 1 tryptophan residue. 53These values are per subunit, which was assumed to be % of the whole protein. The whole protein weighed 217,000 daltons (88). 54 Carbohydrate in residues per 123,500 M,: sialic acid, 4; hexose, 2; acetyl, 12. 55Reported as residues per mole of flavine. 56 integral number of residues: isoleucine, O-l; leucine, O-l; lysine, O-l. 57Residues per molecular weight: glutamic acid, 36-37; valine, 12-13;

methionine, 1-2; leucine, 18-19; mannose, 10; fucose, 3-4; galactose, 1617; IV-acetylglucosamine, 21; uranic acid, 0. 58 Carbohydrates, nearest integral residue: fucose, 1; mannose, 2; galactose, 3; glucose, 3; IV-acetylhexosamine, 4; N-acetylneuraminic acid, 1. 58Carbohydrate content, residues: N-acetylglucosamine, 4; galactose, 3; mannose, 1; glucose, 1; N-acetylneuraminic acid, 2; fucose, 0. B” Amino acid residues: lysine, 14-15; histidine, 3-4; aspartic acid, 22-23; glutamic acid, 35-36; half-cystine, 5-6; tyrosine, 10-l 1 or 12; phenylalanine, 10-11; tryptophan, 3-4. Carbohydrate, percent: mannose, 4.8; galactose, 6.7; IV-acetylglucosamine, 13.4; N-acetylgalactosamine, 1.2; sialic acid, 11.9; fucose, 1.1. 6* Carbohydrate content is reported but how reported (as percent, moles etc.) was omitted. Hexoses, neuraminic acid, and hexosamines were all present. A trace of uranic acid was also present. 62 For every mole of protein: 41 moles of hexose; 29 moles of glucosamine; 18 moles of neuraminic acid. In (101a) the analyses of five variants of or-acid glycoprotein of human serum may be found and in (101b) the analyses of three isoelectric variants are given. 63Carbohydrate content (percent): mannose, 4.1; galactose, 8.1; hexosamine, 7.8; sialic acid, 11.4. 64Carbohydrate content, moles per mole of protein: hexose, 13; acetylhexosamine, 10; acetylneuraminic acid, 6; fucose, 1. 65Carbohydrate content, moles per mole of protein: hexose, 33; acetylhexosamine, 26; acetymeuraminic acid, 16; fucose, 2. 68 Carbohydrate content, moles per mole of protein: hexose, 14; acetylhexosamine, 9; acetyhteuraminic acid, 7; fucose, 1. *’ Carbohydrate content, moles per mole of protein: hexose, 23; acetylhexosamine, 13; acetylneuraminic acid, 7; fucose, 0. 68 Carbohydrate content, mples per mole of protein: glucosamine, 30; sialic acid, 14; mannose, 14; galactose, 14; fucose, 2. 68Carbohydrate content, moles per mole of protein: glucosamine, 22; galactosamine, 0; mannose, 15; galactose, 13; fucose, 2; glucose, 0; sialic acid, 0.

‘O Carbohydrate content, moles per mole of protein: hexose, 15; acetylhexose, 10; acetylneuraminic acid, 6; fucose, 1. ‘I Carbohydrate content, moles per mole of protein: hexosamine, 24; hexose, 26 or 43 (depending on method); sialic acid, 10; fucose, 2. ‘* Carbohydrate content, moles per mole of protein: hexosamine, 29; hexose, 36 or 60 (depending on method); sialic acid, 11; fucose, 73. 73Carbohydrate content, moles per mole of protein: hexosamine, 30; hexose, 34 or 50 (depending on method); sialic acid, 14; fucose, 1. r4 Carbohydrate content, moles per mole of protein: hexosamine, 16; hexose 19 or 33 (depending on method); sialic acid, 9; fucose, 0. r5 Carbohydrate content, moles per mole of protein: hexosamine, 17; hexose, 25 or 36 (depending on method); sialic acid, 6; fucose, 50. 76All exist as cysteine residues. ” Two residues of ornithine reported. ‘* Carbohydrate content, moles per mole of protein: hexose, 43; acetylhexose, 24; acetylneuraminic acid, 17; fucose, 1. ;c, r9 From sequence; the amide ammonia is distributed as 8 asparagine and w 5 glutamine residues. 80From sequence; the amide ammonia is distributed as 12 asparagine and 8 glutamine residues. 81Carbohydrate content, 15%. 8* Carbohydrate content, 23.5%. 83Values rounded to nearest even integer based on Tyr = 28. 20 residues of glucosamine present. 84Present. 8SAll values expressed in relation to aspartic acid as 100. Carbohydrate content, g per 100 g: mannose, 8.7; galactose. 6.3; arabinose, 3.5; glucose, 0.8; fucose, 0.4; xylose, 0.2; glucosamine, 1.8. 88 Neutral sugar content, 1.55%. *’ Neutral sugar content, 1.45%. 88 Neutral sugar content, 0.88%. ag 14-15 residues of glucosamine and 5.9% neutral sugar content.

S+Data calculated on the basis of an observed M, of 20,000 minus the weight due to carbohydrate (2,600). 91In a mixture of hemagglutinin A and B, 2 residues of half-cystine found and 3.3% carbohydrate. 8* Carbohydrate content, residues per mole: glucose, 6; glucosamine, 2. w From sequence; the amide ammonia is distributed as 6 asparagine and 4 glutamine residues. In (127), the amino acid analysis of iron-free hemerythrin is given. 94 Not corrected for destruction during hydrolysis. B5Composition based on 14 aspartic acid residues per subunit. O6In (132) 23 residues of histidine reported. 97 In (132), 18 residues of arginine reported. 9SCarbohydrate content, residues per mole: glucosamine, 2; galactosamine, 1; glucose, 1; galactose, 0; mannose, 2; xylose, I; fucose, 1; sugar “x1’, 3; N-acetylneuraminic acid, 0. 99 Carbohydrate content; residues per mole: glucosamine, 2; galactosamine, 1; glucose, 0; galactose, 0; mannose, 2; xylose, 1; fucose + sugar “x”. 5; N-acetylneuraminic acid, 0. loa See (136) and (137) for slightly different analyses of these hemocyanins and (138) for an analysis of hemocyanin. lo1 4 residues of glucosamine. lo* 3 residues of glucosamine. lo3 Analyses based on assuming 1 residue of tryptophan. lo4 Carbohydrate content, moles per mole: hexose, 40; acetylhexosamine, 27; acetylneuraminic acid, 13; fucose, 2. lo5 This molecular weight is for the protein portion of the molecule and is 78.44% of 69,800 average Mr. Carbohydrate content, residues per molecule: mannose, 17;galactose, 13; glucosamine, 29;N-acetylneuraminic acid, 18. lo6 This molecular weight is for the protein portion of the molecule and is 79.84% of 61,800 average M,. Carbohydrate content. residues per mole-

s P

cule: mannose, 9; galactose, 7; glucosamine, 27; N-acetylneuraminic acid, 19. lo7 Analysis based on 38 lysine residues, 3-4 residues tryptophan. lo8 Analysis based on 34 lysine residues. In (145) may be found analyses for the S forms of hexokinase and earlier analyses for the P forms. lo9 The molar content of amino acids reported were obtained by multiplying the values given in (147)-(149) by 18, i.e., 18 histidines were assumed as the basis of the amino acid analysis. This was suggested in Table II of (148) and Table 2 of (149).

ii0 Amino acid composition based on normalizing values relative to 1 histidine. rlr 3-4 residues lysine. rl* 15 and 19 residues have also been reported (152). II3 18-20 residues of half-cystine. II4 Half-cystine, 6-7 residues; leucine, 52-53 residues; phenylalanine, 26-27 residues. Ii5 Total sugar content, reducing sugar, pentose sugars, and deoxy sugars; zero.

A COMPILATION

OF

REFERENCES

AMINO

ACID

ANALYSES.

VIII

325

FOR TABLES

1. Wengenmayer, F., Ueberschar, K.-H., Kurz. G., and Sund, H. (1973) Elcr. J. Biochem. 40, 49. 2. Wilson. D. B., and Hogness, D. S. (1969)J. Biol. Chem. 244, 2137. 3. Saito, S., Ozutsumi, M., and Kurahashi. K. (1967) .I. Biol. Chem. 242, 2362. 4. Kelly-Falcoz, F., Greenberg, H., and Horecker, B. L. (196S)J. Biol. Chem. 240,2966. 5. Craven. G. R.. Steers, E., Jr., and Anfinsen. C. B. (1965) J. Bioi. Chem. 240, 2468. 6. Johnson, H. N., and Debusk, A. G. (1970) Arch. Biochem. Biophys. 138, 408. 7. Pollard, H. B., and Steers, E. (1973) Arch. Biochem. Biophys. 158, 650. 8. Schade, A. L., and Reinhart, R. W. (1970)Biochem. J. 118, 181. 9. Tang, J. (1970) Methods Enzymol. 19, 406. 10. Tauber, S., and Madison, L. L. (1965)J. Biol. Chem. 240, 645. 11. Bemardin, J. E., Kasarda, D. D.. and Mecham, D. K. (1967) J. Biol. Chem. 242, 445. 12. Platt. S. G., and Kasarda, D. D. (1971) Biochim. Biophys. Acta 243, 407. 13. Heimburger, N., Heide, K., Haupt, H., and Schultze. H. E. (1964) C/in. Chim. Actn 10, 293.

14. 15. 16. 17. 18. 19. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 31. 32. 33. 34. 35. 36. 37. 38. 39. 40.

Cejka. J., and Poulik, M. D. (197l)Arch. Biochem. Biophys. 144, 775. Berggard, I. (1974) Biochem. Biophys. Res. Commun. 57, 1159. Nimberg, R. B.. and Schmid, K. (1972) J. Bio/. Chem. 247, 5056. Iwasaki, T.. and Schmid, K. (1967)J. Biol. Chem. 242, 2356. Lea, 0. A. (1973) Biochim. Biophys. Acta 317, 351. Giogrio, N. A.. Jr., and Tabachnick, M. (1968) J. Biol. Chem. 243, 2247. Slejten. K., Aakisson, I., and Alosaker, J. 0. (1971) Nature New Biol. 231, 118. Sundby, F., and Markussen, J. (1971) Horm. Metab. Res. 3, 184. Bromer, W. W., Boucher, M. E., Patterson. J. M.. Pekar, A. H., and Frank B. H. (1972)J. Biol. Chem. 247, 2581. Sundby, F., Franksen, E. K., Thomsen, J., Kristiansen. K., and Brunfeldt, K. (1972) FEBS Lett. 26, 289. Thomsen, J., Kristiansen, K., Brunfeldt, K., and Sundby. F. (1972) FEBS Lett. 21,315. Li, L. H., Flora, R. M., and King, K. W. (1965) Arch. Biochem. Biophys. 111, 439. Huotari, F. I., Nelson, T. E., Smith, F.. and Kirkwood. S. (1968) J. Biol. Chem. 243, 952. Pazur. J. H., Knull, H. R., and Cepure, A. (1971) Carbohyd. Res. 20, 83. Barker, S. A., Gray, C. J., and Jolley, M. E. (1971) Biochem. Biophys. Rrs. Commun. 45, 654. Pazur, J. H., Knull. H. R., and Simpson, D. C. (1970)Biochem. Biophys. Res. Commun. 40, 110. Hengartner, H., and Zuber, H. (1973) FEBS Lett. 37, 212. Danno. G. (1970)Agr. Biol. Chem. 34, 1795. Pazur, J. H., Kleppe, K.. and Cepure, A. (1965) Arch. Biochem. Biophys. 111, 351. Nakamura, S., and Fujiki, S. (1968)J. Biochem. Tokyo 63, 51. Yoshida, A. (1968) in Hereditary Disorders of Erythrocyte Metabolism (Beutler, E.. ed.). p, 146. Grune and Stratton, New York. Scott, W. A., and Tatum, E. L. (1971) J. Biol. Chem. 246, 6347. Yoshida, A. (1966) J. Biol. Chem. 241, 4966. Rudick, M. .I.. and Elbein, A. D. (1974) Arch. Biochem. Biophys. 161, 281. Rudick, M. J., and Elbein, A. D. (1973) J. Biol. Chem. 248, 6506. Legler, G., von Radloff, M., and Kempfle, ki. (1972) Biochim. Biophys. Acta 257,40. Jacobson, J. W., Strickland. W. N.. and Barrat, R. W. (1969) Biochjrn. Bioph.v.7. Acrti 188, 283.

326

DONALD

M.

KIRSCHENBAUM

41. Strickland, W. N., Jacobson, J. W., and Strickland, M. (1971)Biochim.

Biophys. Acta

251, 21.

42. Blumenthal, K. M., and Smith, E. L. (1973) .I. Biol. Chem. 248, 6002. 43. King, K. S., and Frieden, C. (1970) J. Biol. Chem. 245, 391. 44. Moon, K., and Smith, E. L. (1973) J. Biol. Chem. 248, 3082. 44a. Witzemann, V., Koberstein, R., Sund, H., Rasched, I., Jomvall, H., and Noack, K. (1974) Eur. J. Biochem. 43, 319. 45. Appella, E., and Ton&ins, G. M. (1966) J. Mol. Biol. 18, 77. 46. Landon, M., Melamed, M. D., and Smith, E. L. (1971) J. Biol. Chem. 246, 2360. 47. Sund, H., and Akeson, A. (1964) Biochem. Z. 340,421. 48. Moon, K., Piszkiewicz, D., and Smith, E. L. (1973) J. Biol. Chem. 248, 3093. 49. Switzer, R. L., and Barker, H. A. (1967) J. Biol. Chem. 242, 2658. 50. Miller, R. E., and Stadtman, E. R. (1972) J. Biol. Chem. 247, 7407. 50a. Katunma, N., Katsunuma, T., Towatari, T., and Tomino, I. (1973) in The Enzymes of Glutamine Metabolism (Prusiner, S. and Stadtman, E. R. M., eds.), p. 227, Academic Press, New York. 51. Rowe, P. B., and Wyngaarden, J. B. (1968) J. Biol. Chem. 243, 6373. 52. Woolfolk, C. A., Shapiro, B., and Stadtman, E. R. (1966) Arch. Biochem. Biophys. 116, 177.

53. Shapiro, B. M., Kingdon, H. S., and Stadtman, E. R. (1967) Proc. Nut. Acad. Sci. USA 58, 642. 54. Deuel, T. F., Ginsburg, A., Yeh, J., Shelton, E., and Stadtman, E. R. (1970) J. Biol. Chem. 245, 5195. 55. Sarker, P. K., Fischman, D. A., Goldwasser, E., and Moscona, A. A. (1972) J. Biol. Chem. 247, 7743. 56. Tate, S. S., Leu, F.-Y., and Meister, A. (1972) J. Biol. Chem. 247, 5312. 56a. Tate, S. S., and Meister, A. (1973) in The Enzymes of Glutamine Metabolism (Prusiner, S., and Stadtman, E. R., eds.), p. 77, Academic Press, New York. 57. Ronzio, R. A., Rowe, W. B., Wilk, S., and Meister, A. (1969) Biochemistry 8, 2670. 58. Folk, W. R. (1971) Biochemistry 10, 1728. 59. Adamson, E. D., Szewczyk, A., and Connell, G. E. (1971) Can. J. Biochem. 49,218. 60. Taniguchi, N. (1974) J. Biochem. Tokyo 75, 473. 61. Lapointe, J., and Soll, D. (1972) J. Bioi. Chem. 247, 4966. 62. Massey, V., and Williams, C. H., Jr. (1%5) J. Biol. Chem. 240, 4470. 63. Ida, S., and Morita, Y. (1971)Agr. Biol. Chem. 35, 1550. 64. Majerus, P. W., Brauner, M. J., Smith, M. B., and Minmch, V. (1971) J. Clin. Invest. 50, 1637. 65. Allison, W. S., and Kaplan, N. 0. (1964) J. Biol. Chem. 239, 2140. 66. Smith, C. M., and Velick, S. F. (1972) J. Biol. Chem. 247, 273. 67. Davidson, B. E., Sajgo, M., Noller, H. F., and Harris, J. I. (1967) Nature (London) 216, 1181.

68. 69. 70. 71. 72. 73. 74. 75. 76.

D’Allessio, G., and Josse, J. (1971) J. Biol. Chem. 246, 4326. Jones, G. M. T., and Harris, J. I. (1972) FEBS Lett. 22, 185. Harris, J. I., and Perham, R. N. (1965) J. Mol. Biol. 13, 876. Harris, J. I., and Perham, R. N. (1968) Nature (London) 219, 1025. Suzuki, K., and Imahori, K. (1973) J. Biochem. Tokyo 73, 97. Suzuki, K., and Harris, J. I., cited in Ref. (72). Simpson, R. J., and Davidson, B. E. (1971) Aust. J. Biol. Sci. 24, 263. Greene, F. C., and Feeney, R. E. (1970) Biochim. Biophys. Acta 220, 430. Carlson, C. W., and Brosemer, R. W. (1971) Biochemistry 10, 2113.

A COMPILATION

OF AMINO

ACID

ANALYSES.

VIII

327

77. 78. 79. 80. 81.

White, H. B., and Kaplan, N. 0. (1969) J. Viol. Chem. 244, 6031. White, H. B. (1971) Arch. Biochem. Biophys. 147, 123. VanEys, J., Judd, J., Ford, J., and Womack, W. B. (1964) Biochemistry 3, 1755. Lehmann, F.-G., and Ptleiderer, G. (1968)Hoppe Seyler’s Z. Physiol. Chem. 349,1777. Otto, J., Raggi, A., Machleidt, W., and Bucher, T. (1972) Hoppe Seyler’s Z. Physiol. Chem. 353, 332. 82. Warkentin, D. L., and Fondy, T. P. (1973) Eur. J. Biochem. 36, 97. 83. Fondy. T. P.. Levin, L., Sollohub, S. J., and Ross, C. R. (1968) 1. Biof. Chem. 243, 3148. 84. Fondy, T. P., Herwig, K. J., Sollohub, S. J., and Rutheford, D. B. (1971) Arch. Biochem. Biophys. 145, 583. 85. Ross, C. R., Curry, S., Schwartz, A. W., and Fondy. T. P. (1971) Arch. Biochem. Biophys. 145, 591. 86. Fink, S. C., and Brosemer, R. W. (1973) Arch. Biochem. Biophys. 158, 19. 87. Brosemer, R. W., and Marquardt, R. R. (1966) Biochim. Biophys. Acta 128, 464. 88. Thomer, J. W., and Paulus, H. (1971)3. Biol. Chem. 246, 3885. 89. Heady, J. E., and Kerr, S. J. (1973) J. Biol. Chem. 248, 69. 90. Catsimpoulas, N., Berg, T., and Meyer, E. W. (1971) Znt. J. Prot. Res. 3, 63. 91. Issa, H. A., and Mendicino, J. (1973) J. Biol. Chem. 248, 685. 92. Schuman, M., and Massey, V. (1971) Biochim. Biophys. Acta 227, 500. 93. Rick, P. D., Drewes, L. R., and Gander, J. E. (1974) J. Biol. Chem. 249, 2073. 94. Marchesi, V. T., Tillack, T. W., Jackson, R. L., Segrest, J. P.. and Scott, R. E. (1972) Proc. Nat. Acad. Sci. USA 69, 1445. 95. Walborg, E. F., and Ward, D. N. (1963) Tex. Rep. Biol. Med. 21, 600. 96. Capaldi, R.-A. (1973) Biochim. Biophys. Acra 311, 386. 97. Wagh, P. V., and Roberts, B. I. (1972) Biochemistry 11,4222. 98. Maier, V., and Buddecke, E. (1971) Hoppe Seyler’s Z. Physiol. Chem. 352, 1338. 99. Li, Y.-T., and Li, S.-C. (1970) .I. Biol. Chem. 245, 825. 100. Zito, R., Marcante, M. L., and Caputo, A. (1964) Acta Unio Znt. Contra Cancrum 20, 1146.

101. Marshall, W. E.. and Porath, J. (1964)J. Biol. Chem. 240, 209. 101a. Marshall, W. E. (1966)J. Biol. Chem. 241, 4731. 101b. Ryan, M. F., and Westphal, U. (1972) J. Biol. Chem. 247, 4050. 102. Hao. Y.-L., and Wickerhauser, M. (1973) Biochim. Biophys. Acta 322, 99. 103. Heide, K., Haupt, H., and Schultze, H. E. (1964) C’lin. Chim. Acza 10, 293. 104. Heimburger, N., Haupt, H., Kranz, Th., and Baudner, S. (1972) Hoppe Seyler’s Z. Physiol. Chem. 353, 1133. 105. Schmid, K., and Burgi, W. (1961) Biochim. Biophys. Acta 47, 440. 106. Iwasaki, T., and Schmid, K. (197O)J. Biol. Chem. 245, 1814. 107. Labat, J., Ishiguro, M., Fujisaki, Y., and Schmid, K. (1969)5. Biol. Chem. 244,4975. 108. Grant, D. L., Martin, W. G., and Anastassiadis, P. A. (1967)J. BioL Chem. 242,3912. 109. Ostrem, D. L., and Berg, P. (1974) Biochemistry 13, 1338. 110. Kohn, L. D., Warrennot, W., Carroll, W. R. (1970) J. Biol. Chem. 245, 3821. 111. Little, M., and Williams, P. A. (1971) Eur. J. Biochem. 21, 99. 112. Black, J. A., and Dixon, G. H. (1968) Nature (London) 218, 736. 113. Bamett, D. R., Lee, T.-H., and Bowman, B. H. (1972) Biochemistry 11, 1189. 114. Gordon, S., Cleve, H., and Beam, A. G. (1968) Proc. Sot. Exp. Biol. Med. 127, 52. 115. Cleve, H., Bowman, B. H., and Gordon, S. (1969) Humangenetik 7, 337. 116. Fraser, I. H., and Smith, D. B. (1971) Can. J. Biochem. 49, 141. 117. Keilin, J., (1967) in Structure and Function of Cytochromes (Okunuki, K.. Kamen, M. D., and Sekuzu, I.. eds.), p. 691, Univ. Park Press, Baltimore, Md. 118. Matsumoto, I., and Osawa. T. (1970) Arch. Biochem. Biophys. 140, 484.

DONALD

328 T., N. R. R.

M. KIRSCHENBAUM

119. 120. 121. 122.

Marik, Gould, Poretz, Acton,

Entlicher, G., Kocourek, J. (1974) Biochim. Biophys. Acta 336, 53. R., and Scheinberg, S. L. (1970) Arch. Biochem. Biophys. 137, 1. D., Riss, H., Timberlake, J. W., and Chien, S. (1974)Biochemistry 13, 250. J., Bennett, C., Evans, E. E., Schrohenloher, R. E. (1969)J. Biol. Chem.

123.

Howard, R. K., Sage, H. J., Stein, M. D., Young, N. M., Leon, M. A., and Dyckes, D. F. (1971)J. Biol. Chem. 246, 1590. Toyoshima, S., Osawa, T., Tonomura, A. (1970) Biochim. Biophys. Acta 221, 514. Klippenstein, G. L., Holleman, J. W., and Klotz, 1. M. (1968) Biochemistry 7, 3868. Klippenstein, G. L. (1972) Biochemistry 11, 372. Groskopf, W. R., Holleman, J. W., Margoliash, E., and Klotz, I.M. (1966) Biochemistry 5, 3779. Klippenstein, G. L., VanRiper, D. A., and Oosterom, E. A. (1972) J. Biol. Chem.

244,4128.

124. 125. 126. 127. 128.

247, 5959. 129.

130. 131. 132. 133. 134. 135.

Ferrell, R. E., and Kito, G. B. (1970) Biochemistry 9, 3053. Joshi, J. G., and Sullivan, B. (1973) Comp. Biochem. Physiol. 44B, 857. Ghiretti-Magaldi, A., Nuzzulo, C., and Ghiretti, F. (1966) Biochemistry 5, 1943. Ghiretti, F. (1966) in Physiology of Mollusca (Wilbur, K. M., and Yonge, C. M.. eds.), Vol. II, p. 233, Academic Press, New York. Carpenter, 0. E., and VanHolde, K. E. (1973) Biochemistry 12, 2231. Makino, N. (1971)J. Biochem. Tokyo 70, 149. Dijk, J., Brouwer, M., Coert, A., and Gruber, M. (1970) Biochim. Biophys. Acra 221, 467.

136. Gruber, M. (1968) in Physiology and Biochemistry of Hemocyanin (Ghiretti, F., ed.), p. 49, Academic Press, New York. 137. Witters, R., and Lontie, R. (1968) in Physiology and Biochemistry of Hemocyanin (Ghiretti, F., ed.), p. 61, Academic Press, New York. 138. Claesson, I. M. (1956-1957) Ark. Kemi, 10, 4. 139. Kantor, H. S., Temples, B., and Shaw, W. V. (1972)Arch. Biochem. Biophys. 151, 142. 140. Yoshida, A. (1963) Biochim. Biophys. Acta 71, 544. 141. Hrkal? Z., and Muller-Eberhard, U. (1971) Biochemistry 10, 1746. 142. Tu, A. T., and Friedrich, C. G. (1973) Fed. Proc. (Abstr.) 32, 658, 2506. 143. Carrico, R. J., and Deutsch, H. F. (1969)J. Biol. Chem. 244, 6087. 144. Schmidt, J. J., and Colowick, S. P. (1973) Arch. Biochem. Biophys. 158,458. 145. Gasith, J. G., Schulze, I. T., Gooding, R. H., Womack, F. C., and Colowick, S. P. (1968) Ann. N. Y. Acad. Sci. 151, 307. 146. Meunier, J. C., But, J., and Ricard, J. (1971) FEBS Left. 14, 25. 147. Schwartz, G. P., and Basford, R. E. (1967) Biochemistry 6, 1070. 148. Chou, A. C., and Wilson, J. E. (1972) Arch. Biochem. Biophys. 151, 48. 149. Easterby, J. S., and O’Brien, M. J. (1973) Eur. J. Biochem. 38, 201. 150. Sullivan, J. O., and Ikawa, M. (1973) Biochim. Biophys. Acta 309, 1 I. 151. Markwardt, F., and Walsmann, P. (1967)Hoppe Seyler’s Z. Physiol. Chem. 348, 1381. 152. Rechler, M. M. (1969)J. Biol. Chem. 244, 551. 153. Klee, C. B., and Gladner, J. A. (1972) J. Biol. Chem. 247, 8051. 154. Sokhina, A. M. (1968) Biochemistry (Biokhimya) 33, 424. 155. Recsei, P. T., and Snell, E. E. (1973) Biochemistry 12, 365. 156. Loper, J. C. (1968)J. Biol. Chem. 243, 3264. 157. Henderson, G. B., and Snell, E. E. (1973)J. Biol. Chem. 248, 1906. 158. DeLorenzo, F., DiNatale, P., and Schechter, A. N. (1974) J. Biol. Chem. 249, 908. 159. Kalousek, F., and Konigsberg, W. H. (1974) Biochemistry 13, 999. 160. Wuu. T. C., and Saffran, M. (1969) J. Biol. Chem. 244, 482.

A COMPILATION

OF AMINO

ACID

ANALYSES.

VIII

329

161. Schanbacher, F. L., Lee, C. K., Wilson, I. B., Howell. D. E., and Odell, G. V. (1973) Comp. Biochem. Physiol. 44B, 389. 162. Nakos, G., and Mortenson, L. E. (1971) Biochemistry 10, 2442. 163. Haschke, R. H., and Campbell, L. L. (1971)J. Bacterial. 105, 249. 164. Noyes, B. E., and Bradshaw, R. A. (1973) .I. Biol. Chem. 248, 3052. 165. Menzel, H. M., and Hammes, G. G. (1973) J. Biol. Chem. 248, 4885. 166. Helmkamp, G. M., Jr., and Bloch. K. (1969)J. Biol. Chem. 244, 6014. 167. Kohn, L. D., and Jakoby, W. B. (1968) J. Biol. Chem. 243, 2494. 168. Jarabak, J., and Street, M. A. (1971) Biochemistry 10, 3831.

ACKNOWLEDGMENTS The prime source of data were the journals and books of the Library of the Downstate Medical Center, and I thank the librarians for the pleasant and very necessary assistance. A secondary source of data was the Library of the Marine Biological Laboratory, Woods Hole, MA, where I have spent the last few summers (1971-1974) in a delightful combination of business and pleasure. I also thank Miss Margo Colindreler for her assistance in the typing of this manuscript and Mr. Edward Becker for assistance in checking the references.