ANALYTICAL

66, 123- 150 ( 1975)

BIOCHEMISTRY

A Compilation

of Amino VII.

Residues

Acid per

Analyses

of Proteins

Molecule-5

DONALD M. KIRSCHENBAUM Depuriment of Biochemistry, College of’ Medicine, Downstate Medical Center, Brooklyn, New York 1120.3 Received

July

3 1, 1974:

accepted

December

11. 1974

This paper is the fifth in the series reporting the number of residues per molecule of protein (l-4). The dictates laid down in the previous papers have been followed in this one, i.e., molecular weights under 10,000 rounded off to the nearest hundred and to the nearest thousand for weights over 10,000. The number of residues have been rounded off to the nearest integral number. Most of the data reported were obtained by column chromatographic methods applied to acid hydrolysates. The determination of cysteine, tyrosine, and tryptophan were occasionally done by colorimetric or spectrophotometric methods. (See refs. l-3 for references to methods). The remainder of the data was taken from sequences reported for the proteins. This allowed the assignment of the number of residues of asparagine and glutamine to be made and this information along with the amounts of e-N-substituted lysines is reported in the footnotes to Table 2. Table 1 is the Protein Index and gives the names of the proteins, the sources of the proteins, and if the proteins are enzymes the Enzyme Commission numbers. Table 2 gives the amino acid analyses as residues per molecular weight of protein, amide ammonia, molecular weight, and literature citation. Aspartic acid includes asparagine and glutamic acid includes glutamine. Where the results have been taken from sequence analysis, no mention has been made of amino acid determination by column chromatography. Usually this information is also present in the same paper and should be consulted if a comparison is desired between amino acid content from sequence and amino acid content by column chromatographic analysis. 123 Copyright All rights

0 1975 by Academic Press, Inc. of reproduction in any form reserved.

DONALD

124

M. KIRSCHENBAUM

REFERENCES 1. 2. 3. 4.

Kirschenbaum. Kirschenbaum, Kirschenbaum, Kirschenbaum,

D. D. D. D.

M. M. M. M.

(1971) (1972) (1973) (1974)

Anal. Anal. Anal. Anal.

Biochem. Biochem. Biochem. Biochem.

44, 49, 52, 61,

159. 248. 234. 567.

ACKNOWLEDGMENTS The prime source of data was the Library of the Downstate Medical Center and I thank the librarians for their pleasant and very necessary assistance. I thank the librarians of the Library of the Marine Biological Laboratory, Woods Hole, Mass., for their assistance during the past few summers. I was a Library Reader there and compiled some data during those lovely summer months. I thank Miss M. Colindreler for typing the manuscript and Mr. E. Becker for checking the references.

AMINO

ACID

ANALYSES

OF PROTEINS

TABLE PROTEIN

I Name: Source: 2 Name:

Deoxyribonuclease II Pig Deoxyribonucleic acid ligase

Source: 3 Name:

E. coli

5 6 7 8 9 10

11 12

13 14 I5 16

Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:

17 Name: Source:

Dihydrolipoamide dehydrogenase E. co/i K12 Dihydrolipoyl transsuccinylase E. co/i

E3 Immunity substance E. co/i

E3 Immunity protein E. coli W31 IO (E3) Edestin, A chain Plant Edestin, B chain Plant Elastase Pig Elastase Pseudomonas

Acrocylindrum

Enolase E. coli

Enolase Rhesus monkey (Macaca mulatta) Enolase Rainbow trout (Salmo gairdnerii)

Enolase Pig kidney Enolase Thermus

X-l

Enterotoxin Staph.

21 Name: Source: 22 Name: Source: 23 Name: Source: 24 Name: Source: 7-5 Name: Source: 16 Name: Source: 27 Name: Source: 28 Name: Source: 29 Nume: Source: 30 Name: Source:

aureus

A

Enterotoxin Staph.

c

Enterotoxin Staph.

c strain 361

aureus

Enterotoxin Staph.

strain I37

aureus

E

aureus

FRl-32

Erabutoxin a Laticauda

semifasciata

Erabutoxin b Laticauda

semifasciata

Erabutoxin c Laticauda

semifasciuta

Erythrocuprein Human erythrocyte Erythrocuprein Human erythrocyte Erythrocuprein Human erythrocyte Erythrocruorin Annelid worm (Cirruformia grandis)

31 Name:

Esterase. arginine-ester hydrolyzing enzyme Broadbanded copperhead snake venom (Agkistrodon

32 Name:

Ethanolamine

Source: 33 Name: Source: 34 Name: Source: 35 Name: Source: 36 Name: Source: 37 Name: Source. 38 Nume: Source. 39 Name: Source: 40 Name: Source. 41 Name: Sours:

Clostridial

aeruginosa

Elastin, salt soluble Pig aorta, copper-deficient Encephalitogenic protein, basic, fr. 4 Human brain Endolysin k Phage Endonuclease

(gairdnerii 18 Name: Source: 19 Name: Source: 20 Name: Source:

1 INDEX

Number

Number

Source: 4 Name:

125

VII

contortrix

laticinctus)

deaminase

Estradiol dehydrogenase Human placenta Exopenicillinase Type A Staphylococcal

Exopenicillinase

Type B

Staphylococcal

Exopenicillinase

Type C

Staphylococcal

Factor IlIla’ Staph.

aureus

Factor Bovine Factor Bovine Factor Bovine Factor Bovine

IX. clotting plasma X, clotting plasma X,. clotting plasma X2. clotting plasma

126

DONALD

M.

TABLE Number

1 (Continued) Number

Factor Bovine Factor Bovine ,Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor Factor chain Source: Factor 60 Name: Factor peptide Source: Factor 61 Name: Factor Source: Human 62 Name: Factor

42 Name: Source: 43 Name: Source: 44 Name: Source: 45 Name: Source: 46 Name: Source: 47 Name: Source: 48 Name: Source: 49 Name: Source: 50 Name: Source: 51 Name: Source: 52 Name: Source: 53 Name: Source: 54 Name: Source: 55 Name: Source: 56 Name: Source: 57 Name: Source: 58 Name: Source: 59 Name:

Source: 63 Name: Source:

KIRSCHENBAUM

X,, clotting plasma XZ, clotting plasma X, activated: X,“” X, bovine X, activated: X,‘” X, bovine X, activated: X,rMET X, bovine X, activated: XaTF X, bovine X, activated: XaRVV X, bovine X, activated: X,aW X, bovine X, activated: X,a”” X, bovine X,, heavy chain X,, bovine X,, light chain X,, bovine X,, heavy chain X2, bovine X,, light chain X,, bovine X1, heavy chain XI, bovine X1, light chain X,, bovine X,, heavy chain X,, bovine X?, light chain X,, bovine X,, (RVV) heavy

64 Name: Source:

Factor, direct lytic Ringhals venom (Haema-

65 Name: Source: 66 Name: Source:

Factor 2, elongation Rat liver Factor, epidermal growth Mice, submaxillary gland adult albino Factor, epidermal growth Mice, submaxillary gland adult albino Factor, gelling Squash (Curcubita pepo) phloem sieve tube Factor, hemolytics Bull seminal vesicle Factor 1, host, required replication of QP RNA

charus

67 Name: Source: 68 Name: Source: 69 Name: Source: 70 Name: Source: 71 Name: Source: 72 Name: Source: 73 Name: Source: 74 Name: Source: 75 Name: Source: 76 Name: Source: 77 Name:

X,, (RVV), bovine X,, (RVV) activation X,, (RVV), bovine XIII plasma . TS

E. coli

Factor, calcium-sensitizing Rabbit skeletal muscle

Source: 78 Name: Source: 79 Name: Source: 80 Name: Source:

haemachates)

of 2 of

for

E. coli

Factor F,, initiation E. coli Q13 Factor, inhibitory (37,000 daltons) Rabbit skeletal muscle Factor, inhibitory (23,000 daltons) Rabbit skeletal muscle Factor, inhibitory (14,000 daltons) Rabbit skeletal muscle Factor, Vitamin B,, intrinsic Human gastric juice Factor, intrinsic (Vitamin Bd Human gastric juice Factor lethal for organisms with disturbed cortisone production Staphylococcal

Factor, nerve growth Mouse, submaxillary gland Factor, nerve growth Mouse, submaxillary gland Factor, nerve growth Snake venom (Vipera russelli)

AMINO

ACID

ANALYSES TABLE

Source: 82.

Name: Source:

Number Factor, somatropin-release inhibitory Sheep hypothalamus Factor 1, SPO 1 transcription SPOI-infected Bacillus subG/is

83 84

Name: Source: Name: Source:

Fatty acid synthetase Chicken liver Fatty acid synthetase Pigeon liver Ferredoxin I

85

Name:

Azotobacter

86

Source: Name: Source:

Bacillus

81

Name: Source:

Ferredoxin

88

Name: Source:

Ferredoxin Yellow green alga

Clostridium

Name: Source:

Azoferredoxin

102

Name: Source:

Ferredoxin

103

Name:

Ferredoxin

104

Source: Name:

Ferredoxin

Source:

Leucaena

Nume: Source:

Ferredoxin

105

1

106

Name:

107

Source: Name:

polymyxa

II

Source:

polymyxa

Name:

Ferredoxin

Source:

Chlorobium tophilum

90

(Bumil-

108

thiosulfa-

Ferredoxin Chloropseudomonas

ethy-

111

licum

91

Name:

Ferredoxin

Source:

Chlorobium tophilum

92 93

Name:

Ferredoxin

Source:

Chromatium

Name: Source:

desulfuricans glauca

Methanobacterium

ome-

Ferredoxin Micrococcus

aerogenes

Ferredoxin Blue-green alga

(Micro-

Ferredoxin

Name:

Ferredoxin

Source:

Rhodospirillum

Source: Name: Source:

112 thiosulfa-

Name: Source:

Tassajara

1

Rhodospirillum

rubrum

II rubrum

Ferredoxin Spirochaeta

aurantia

Ferredoxin Green alga Ferredoxin Thermophilic choccus

(Scenedesmus)

alga (Syne-

lividus)

Ferredoxin

114

Name:

Clostridium ihermosaccharolyticum

I 15

Source: Name:

tartarivorum

116

Source: Name:

butyricum

117 Name:

pasteurianum

118

acidi-urici

119 Name:

Ferredoxin Alfalfa Ferredoxin Fern Ferredoxin Amaranthus Ferredoxin Horse tail leaves Ferredoxin Spinach Ferredoxin Taro (Colocasia esculenta) Apoferritin Horse spleen Apoferritin Horse spleen Apoferritin Horse liver

Clostridium

Name: Source:

Ferredoxin Ferredoxin

97

Name: Source: Name:

Clostridium

98

Source: Name:

99

Source: Name:

100

Desulfovibrio

Ferredoxin

Ferredoxin

96

$gas

Name: Source:

Name:

95

Desulfovibrio

113

Source:

94

pasteurianum

Name: Source:

110 Name:

8327

Name:

Clostridium

cysti.,)

109

Source:

pasteurianum

lianskii

vinelandii

Ferredoxin

Bacillus

Source:

101

leriopsis) 89

127

VII

1 (Continued)

Number 81 Name:

OF PROTEINS

Clostridium Clostridium

Source:

Ferredoxin

Source:

Molybdoferredoxin Clostridium

Source: Name:

120

pasteurianum

Molybdoferredoxin. subunit

Source:

Clostridium

Name:

Molybdoferredoxin, subunit

60,000 121

pasteurianum

50,000

122

Source: Name: Source: Name: Source: Name: Source:

Veilonella

alcalescens

128

DONALD

M. KIRSCHENBAUM

TABLE Number 123 Name: Source: 124 Name: Source: 125 Name: Source: 126 Name: Source: 127 Name: Source: 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 Name: Source: 142 Name: Source: 143 Name: Source: 144 Name: Source:

145 Name: 146

Source: Name: Source:

1 (Continued) Number

Apoferritin Human spleen Apoferritin Human liver Apoferritin Tadpole red cell Fetuin Lamb Fetuin Fetal calf serum Fibrin Human Fibrin Bovine Fibrin, a-polymer Human Fibrin S-chain Human Fibrin y-dimer Human Fibrinogen Human Fibrinogen Human Fibrinogen I, Human Fibrinogen I, Human Fibrinogen Human Fibrinogen, A-chain Human fibrinogen Fibrinogen, B-chain Human fibrinogen Fibrinogen, C-chain Human fibrinogen Fibrinogen, o-chain Human fibrinogen Fibrinogen, P-chain Human fibrinogen Fibrinogen, y-chain Human fibrinogen Fibrinogen Bovine Fibrinogen, or-chain Bovine fibrinogen Fibrinogen, P-chain Bovine fibrinogen

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: Source: 158. Name: Source: 159. Name: Source: 160. Name: Source: 161. Name: Source:

162. Name: Source:

Fibrinogen, y-chain Bovine fibrinogen Fibrinogen B Lobster Ficin Ficus

glabrata

Ficin B Ficus

glabrata

Ficin E Ficus

glabrata

Ficin F, Ficus

glabrata

Ficin F, Ficus

glabrata

Ficin H Ficus

glabrata

Ficin component C Ficus

carica

Ficin component D Ficus

carica

Ficin Ficus

glabrata

Flagellin Bacillus Bacillus Proteus

IF05988

Proteus

vulgaris

Purdue

strain Flagellin Proteus

Source:

Salmonella

164. Name:

Flagellin

Source:

Salmonella

165. Name:

Flagellin

Source:

Salmonella

166. Name:

Flagellin

Source:

Salmonella

168. Name:

vulgaris

Flagellin

Flagellin

Source:

subtilis

Flagellin

163. Name:

167. Name:

KM

megaterium

Flagelhn

mirabilis serpens adelaide ad&aide SJ25

Flagellin, P-filaments Flagellin of Salmonella SJ25 Flagellin

Source:

Salmonella typhimurium

169. Name:

Flagellin

para-

SL877

AMINO

ACID

ANALYSES

TABLE Number Source: 170.

Name: Source:

171.

Name: Source:

172.

Name: SolaTe:

174.

Sulmonella

175.

Salmonella typhimurium

176.

177.

source:

178. Nume: Source:

179.

Name: Source:

SLI 69 typhimurium

SL87 1 Flagellin

Name: Source:

181. Name: Source: 182.

Name: Source:

183. 184. 185.

Name: Source: Name: Source: Nome: Source:

Name: Source:

187. Name: Source: 188. Name: 189.

typhimurium

para-

Desulfovibrio

SL877

Flagelhn Arizona

Salmonella typhimurium

Source:

E. coli

Source:

SLl61

196.

Name: Source:

197. Name:

para-

SL174

Flagellin

Source:

Salmonella typhimurium

198.

para-

Name:

SL168

Flagellin Salmonella

para-

Salmonella

para-

Salmonella

essen

SL.588

Source: Nume:

202.

Source: Name:

Source: 204.

Name: Source:

205.

Name: Source:

MP

Flavodoxin

206.

Name: Source:

nidulans

vinelandii

N-Formimino-L-glutamate iminohydrolase Pseudomonas sp. Formyl tetrahydrofolate synthetase

201.

Flavodoxin Clostridium

Flavodoxin

Candida

senftenberg

SL736 Flagellin

alga (Sym-

lividus)

Azorobacter

Source: Name:

Source:

rubrum

Flavodoxin Thermophilic

200.

203. Name:

Salmonella

Rhodospirillum

Clostridium

SL166

Flagellin

e/sdeni/

Flavodoxin

Source: Name:

abortus-equi

SL23 Flagellin Salmonella typhimurium

Flavodoxin Peptostreptococcus

199.

SL 165

Flagellin

vulgaris

Flavodoxin

choccus

Flagellin

Anacystis

Source: Name:

vulgaris

Miyazaki Flavodoxin Desuljovibrio

para-

Salmonella typhimurium

Desulfovibrio

192.

195.

vulgaris

Flavodoxin

Name:

SL642

arizona

(Strain 137) Flagellin

gigus

Flavodoxin

Source: Name:

193. Name: Source: 194. Name:

jusc,a

Flavodoxin

191.

Flagellin Salmonella typhimurium

Chlorella

Source: Name:

pasteurianum

Flavodoxin

Desulfovibrio

Source:

para-

SL 161

Flavodoxin Clostridium

Source: Name:

180

fyphimurium 180.

186.

190.

Salmonella

Salmonella typhimurium

Name:

129

VII

1 (Continued)

Flagellin

Flagellin

Nume: Source:

para-

Salmonella

Name:

Nnme: Source:

typhimurium

SW1061 Flagellin

Source: Name: Source:

PROTEINS

Number

SWI 173.

OF

acidi-urici

Fructose 1,6-diphosphatase utilis

Fructose 1.6-diphosphatase Spinach chloroplast Fructose 1.6-diphosphatase Rabbit muscle Fructose I ,6-diphosphatase Rabbit liver Fructose 1.h-diphosphatase Bovine liver Fructose 1,6-diphosphatase Pig kidney or-Fucosidase Rat epididymus Fumarase Pig heart

acid

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

Amino

453 1

37 25 22 38 7 29 36’ 17’ 31 36 10 31 18 15 9 19 15 18 -2

1

51 67 66 71 28 34 30 36 56 88 8 10 32 42 15 26 8 7 74 2

2

58 59 49 38 42 26 19’ 28r 45 53 2 10 41 16 13 16 10 56 3

3

27 40 31 39 17 18 28 24 39 41 0 12 22 22 6 9 7 5 42’ 4

4

RESIDUES

8 2 6 6 3 3 6 2 18 10 14 1 5 1 1 8 4 6

5

Residues

6

20 13 14 15 12 8 16 8 29 46 3 3 4 27 5 8 7 2 29 28 7

7

2

I1 16 15 15 8 7 11 8 22 21 2 5 6 18 3 9 6 2 11 21 7

per molecular

8

index

WEIGHT

Protein

TABLE MOLECULAR

7 1 6 6 3 3 6 2 17 8 1 1 5 1 1 8 4 2 -

5

PER

25 17 27 18 10 7 22 19 24 19 8 2 3 12 6 3 I1 7 335 8

weight

9

numbers

39 32 20 15 10 12 26 20 49 20 5 9 12 16 7 19 24 5 21 406 9

11

287 203 116 40 14 92r 10’ 131 3 15 38 4 23 14 74 10

of protein

10

OF PROTEIN

11

26* 12 4 8 4 13 15 8 12 10 12 16 10 8 4 -

12

12

15 13 7 14 9 5 9 6 19 16 1 3 12 12 3 5 5 3 -9 -

13

13

10 19 12 13 5 11 26 18 26 7 2 0 9 8 310 3 4 10 -

14

90 116 48 58 64 22 42 41 85 91 3 21 75 21 14 24 21 3 -11 901 14

15

67 78 48 63 39 33 37 29 81 71 10 13 61 30 14 21 18 6 82 15

16

w’ 0

Glycine Alanine Vaiine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x 1O-3 Ref.

Amino acid

69 80 56 64 56 30 50 33 104 78 12 14 72 33 14 26 20 6 -

881 17

92' 16

18

81 92 56 67 56 31 49 33 99 89 8 12 80 24 21 28 22 3 ‘* -

17

382' 18

-

120 16

71

68 230 185 47

0

358 367 273 319 228 97 161 167 382 463

19

12 8

18 18

10 4

10 53 24 2'3

8 38 4 7 12 21 2 36' 34 20

17 38 27 2 ‘I3

2 25 7 7 8 19 2 31 28l 19

8 14 25

18 9 22 20

21

15

20 23

24

25

26

27

20 54 24 2'3 9 37 4 7 12 21 2 34' 34 20

19

8

12

17 8 20 18

25 8 7 9 18 2 30' 30 21

1

18 38 28 2

16

6

11

13 26

10

21

6.8 22

1 1 8 I4

2

1

4 3

8 *3 0

7'5 6.9 22

1 1

4 3 2 2

0

5 4 8 8 I3

8

4 4

1

4 4 8 5 5 8

2

1

5 0

2

5 0

8 I4 6.8 22

1 1

3 3 2 2

0

818

8

4 4 8 5 5

I

2

5 0

17

28l6 34 23

0 0

23 9 17 9

0

40 28 5

34 24

-17

23 8 13 9

-

20 16 36 27 7

11

11 20

47 21 30 19 17

28

52 21 28 20 16

Residues per molecular weight of protein

22

Protein index numbers

0

25

-18 -

3

0

20 8 14 8

-

38 27

15

19

11

13

18

60 23 26

29

5

17 26

-19

2

9

10 2

6

0

22 15 5

30 27

3 3 4

5

21 31 13 23 35 9 3 9 4

11 18 10

11 14 6 5 8

87 26

31

12 17

30

29 28

-

13 23 20 3 6 19 9 4 7 7 4

11

7

18 20 14

19 19

32

w

acid

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

Ammo

13 19 13 22 17 10 18 13 40 18 0 2 42 5 2 7 11 _

30 30

34 29

34

31 36 32 41 4 19 19 16 21 28 6 4 10 22 7 13 6 I -120

33

30 30

16 21 11 22 15 11 17 12 42 22 0 2 43 5 2 7 9 -

35

30 30

1.5 19 11 23 18 10 17 11 39 18 0 2 45 4 3 7 14 -

36

36 31

2421 51 9 39 15 3 12 15 33 45 32’ 15 18= 12 12 15 6 0 -1

37

55 32

30 19 25 19 19 13 29 20 36 47 17= 3 28 17 8 15 9 11 -22

Residues

38

TABLE

55 33

45 34 28 33 13 21 33 33 44 68 24 6 21 26 11 23 10 13 -1

39 40

index

49= 34

41 31 24 32 11 20 29 30 40 61 24 6 21 25 10 21 9 -I

per molecular

Protein

2 (Continued)

41 31 25 30 11 20 29 30 40 61 24 6 21 25 11 21 10 -1 4924 34

weight

41

numbers

55 35

38 30 26 30 12 18 29 30 40 56 19 6 22 25 10 20 9 10 -25

of protein

42

37 29 27 31 12 18 30 28 39 57 19 6 22 25 11 20 9 9 -26 55 35

43

37 24 23 23 10 10 26 24 33 58 22 6 23 24 9 20 9 9 -1 50 36

44

38 25 24 25 11 11 24 26 38 60 23 6 24 24 9 21 10 -1 50 36

45

38 24 24 25 11 10 23 24 39 60 19 6 24 24 9 24 10 -1 50 36

46

38 25 24 23 11 10 20 26 37 59 24 6 24 23 9 22 10 -1 50 36

47

50 37

43 28 27 22 12 12 27 30 38 59 26 6 27 28 10 23 11 9 -

48

acid

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

Amino

53 34 27 28 12 14 33 31 44 68 18 6 30 28 11 25 12 50 38

49

40 26 28 25 12 15 25 30 40 64 26 6 27 25 10 22 11 50 39

50

13 6 5 7 2 3 9 6 14 25 14 trZ7 7 7 3 7 2 -1

15 34

39 34

52

29 24 19 22 9 15 20 21 27 36 11 3 16 18 8 13 7 -128

51

39 34

28 25 19 23 9 17 17 22 27 34 10 2 14 19 8 13 7 -129

53

15 34

13 6 5 7 2 3 11 6 15 25 13 I 6 7 3 8 3 -1

Residues

54

38 35

28 23 23 23 10 17 19 22 27 36 9 5 15 18 7 10 6 7 -30

55

56

index

17 35

17 9 6 8 2 3 12 7 15 33 16 0 7 8 3 8 3 1 -31

per molecular

Protein

38 35

26 23 21 23 9 16 21 24 27 34 9 5 15 17 8 13 7 8 -32

weight

57

numbers

17 35

15 6 6 7 2 3 11 7 15 29 15 0 7 8 3 8 3 2 -33

of protein

58

27 35

22 18 20 15 8 12 12 19 18 25 8 5 14 14 6 13 6 5 -34

59

11 35

6 6 5 7 2 5 7 4 10 9 1 0 0 4 2 1 3 2 -35

60

200 107 188 196 119 150 196 178 265 304 78 46 167 129 61 105 135 57 32036 40

61

30 35 28 14 14 8 7 12 25 49 1 8 20 8 3 8 1 28 41

62

18 42

11 14 8 10 8 4 7 5 20 35 2 7 10 8 2 8 2 0 --I

63

7 43

2 1 4 638 2 5 3 3 6 1 S3’ 2 10 1 1 1 1 0 -

64

acid

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

Amino

84 77 79 86 62 52 59 49 92 107 22 30 76 52 18 40 25 8 -8 44

65

6 0 2 4 2 2 6 2 739 339 640 1 0 4 1 0 5 2 -1 6.0 45

66

46

6 0 2 3 2 2 6 2 7 3 6 1 0 3 1 0 5 2

67

25 14 33 39 34 14 20 7 35 46 6 3 41 17 10 22 13 lj’ 63 -1 47

68

/-I --I 8 48

5 4 4 3 1 6 4 3 8 7 5 1 5 3 1 4 5

69

13 49

-

1 4 4 4 3 3

8 6 8 7 4 4 14 6 10 13 -

Residues

70

TABLE

72

index

11 34 14 24 9 11 11 7 27 76 1 6 43 27 6 6 5 37 51

per molecular 4 7 7 4 3 1 4 5 8 9 1 1 10 8 1 2 3 1 10 9.4 50

71

Protein

2 (Continued)

-

-

10 17 9 20 5 6 10 4 19 38 3 9 24 15 4 3 3 23 51

weight

73

numbers

14 51

-

7 11 5 12 5 4 6 6 13 18 0 3 17 9 2 3 2

of protein

74

34 38 38 54 33 37 49 39 57 60 32 1.5 25 8 7 17 18 6 -42 66 52

75

24 23 24 30 20 32 33 26 37 36 12 8 16 6 5 9 10 43 -1 53

76

21 7 3 2 1 5 2 2 3 5 0 3 3 0 1 10 54

17

5 8 13 3 5 2 11 14 11 8 6 1 8 7 4 7 2 3 944 139 55

78

13 19 29 8 12 5 23 30 25 20 1045 2 19 16 8 16 4 6 24 30 56

79

13 14 33 7 12 14 16 22 44 15 12 6 14 15 6 12 7 12 -46 37 57

80

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x IO-” Ref.

Amino acid

-

96 119 91

93

17

0

2

14

2 0

4

1 0 -1 12

2"

0 2 0 0

3

0 I I”

58

-9

181 164'

12

177 143

9

59

60

-

117 107 56 362'

-

306 407

540 61

345

-

305 413 56 62

164

198 164 232

288 408

7

4

5

430 168 183 276 180

282 27.5

11 8

9

291

6

I 0

288 300

84

2

83

7

82

1 I 0 0 0 0 1

81

62

5 2 1 21’ 14

2

I

6

1

20 8

4 15

9 2

8 7

10

8

4

85

87

63

8.8

4

1 0 2

63

8.8

1 0 5 2 -

6

1

4

4

--AX

4 3 6 3

5

6

9 9 4

5

6 4 3

3 4

15 8

-

88 89

90 91

64

0

3 4

1 5 I 1

4

15

14

6

I

5 3

6 9

65

-1

0

3

-49 0 0 0 0 0

3 9

3

4 3

4

2

4

65

-1

0

3

Y 8 0 0 0 0 0

-50

3 2 4

4

5 2

66

-

2 0

1

-51 -51 0 0 0 0

3

4 4 2 4

1

3

Residues per molecular weight of protein __-__ -51 6 8 6 4 4 7 11 8 9 9 11

86

Protein index numbers

67

8.9

7%

0

3

1 2 2 2 0

9

8 16

4 6

5

6

3 6 3

5

92

6 68

09

0 2 0 1 0

2

0

4 7 8

4

0 5

0 5 2 1

69

6

0 0 0 I 0 2 53

2

0

7 8

4 4

1

2

4

5 10

95

4

5 10

-~

93

70

6.1

7 54

0

2 2

0 0

9 5 8 0 0

3 3 3

6 0 4

5 7

95

5 5s 71

-

1 0

1

1 0 0

0

4 8

8

1

3 5

0 5

8 6

4

96

acid

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

Amino

91 70 74 69 80 43 46 60 96 98 20 30 80 31 23 34 42 3 -1

110 73

4 9 6 0 5 4 3 1 8 4 8 0 0 1 0 0 2 0 356

72

98

60 73

54 40 42 33 42 23 26 32 59 59 9 18 47 16 16 19 20 -1

99

50 73

41 29 27 30 34 26 22 27 42 45 8 12 43 16 12 16 17 -1

100

55 73

62 40 12 52 34 18 24 24 45 70 34 16 32 24 4 11 18 0 -

101

75

74

-9

-

6 2 5 2 4 3 2 3 10 -58 6 0 2 0 1 0 0 0

104

index

459

76

-

6 7 6 10 4 S 7 4 I1 16 5 0 5 2 1 3 3 1

per molecular

103

Protein

2 (Continued)

1 6 5 1 5 4 2 0 11 10 6 2 1 1 0 1 0 0 1157 -

Residues

102

TABLE

77

(j

6 14 5 0 0 2 2 1 3 5 5 0 2 0 0 0 2 0 -

weight

105

numbers

78

-

4 7 4 0 6 5 5 0 8 4 8 0 1 0 0 0 2 0 560

of protein

106

79

6 8 5 9 6 4 7 6 11 11 5 1 3 2 2 2 4 1 -

107

80

4 7 7 3 6 -61 3 4 9 12 6 -62 4 1 3 0 0 -

108

80

4 6 6 4 4 4 2 -63 10 8 3 -62 5 1 0 1 2 -

109

5 81

-

3 8 4 1 4 5 3 2 8 6 6 0 3 0 0 1 2 0

110

7 10 5 7 3 4 8 10 12 10 6 1 4 1 1 3 4 0 464 82

111

6 6 7 10 4 5 4 6 11 17 5 0 4 3 1 3 4 0 83

112

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x IO-” Ref.

Amino

5 5 3 0 6 2 7 2 5 6 8 1 2 1 0 0 2 0 -9 84

113

11 85

7 9 9 6 4 3 8 6 9 16 5 0 5 1 2 2 4 I 3 65

114

86

9 7 5 7 6 -66 -67 6 14 9 5 2 4 1 2 4 3 0 -

115

-

86

6 10 5 6 6 -66 8 8 12 14 5 I 4 1 1 I 4 I

116

87

-

4 I 4 I I 4 2 0

9 6 6 8 5 4 8 7 -68 -68

117

II 88

6””

6 9 7 8 4 4 7 8 13 13 5 0 4 I 1 2 4 1

Residues

118

9 6 10 6 4 4 8 6 10 15 5 0 5 1 1 2 4 1 6”’ 89 140 435 577 -71 -71 195 213 -71 175 134 -71 453 ’ 480 90

250 348 173 -71 -71 -71 -71

per molecular

Protein index -__ 119 120

19 91

19 91

-

2

2

-

10 13 7 24 4 3 9 6 18 25 3 3 9 9 7 8 4

19 91

11 14 6 23 4 4 8 6 19 22 2 3 10 9 7 7 4 2 -

__-__123

of protein

122

10 14 7 25 4 3 9 6 17 24 3 3 9 IO 6 7 5

weight

121

numbers

19 91

10 14 6 23 3 3 9 6 19 24 2 3 10 8 5 7 6 2 20 92

16 15 10 17 6 4 15 8 21 24 0 4 13 7 6 7 5 4 49 93

25 40 38 28 14 35 22 20 32 38 12 16 II 11 12 8 2 -72 48 94

2 241

7

24 33 40 27 15 34 26 25 33 34 12 0 16 12 10 I1

305 144 143 192 134 162 248 235 362 317 58 51 197 141 61 94 106 72 312 340 95

128

acid

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

Amino

285 131 138 177 127 110 244 209 349 318 56 60 208 146 62 88 99 77 291 340 95

129

47 28 26 34 17 36 33 27 59 61 -

36 26 8 13 22 60 96

43 38 16 22 15 73 96

131

74 29 31 37 21 45 69 55 64 70 -

130

37 11 10 21 21 53 96

43 30 16 31 22 24 30 36 57 55 -

132

281 142 134 177 105 150 251 192 346 339 20 64 197 146 59 93 101 78 314 32373 97

133

293 143 138 183 128 150 231 180 361 299 56 63 184 128 56 94 104 71 252 340 95

135

136

index

199 111 102 134 80 103 166 134 270 241 45 48 161 119 38 65 78 53 229 269 98

per molecular

Protein

2 (Continued)

273 143 113 158 97 132 244 184 303 302 65 62 202 151 51 88 97 65 280 325 98

Residues

134

TABLE

288 143 144 175 117 139 202 176 359 329 72 64 215 155 59 99 101 51 333 99

weight

137

numbers

35 22 18 24 18 18 22 22 51 44 8 7 33 18 9 14 17 5 47 99

of potein

138

46 30 24 30 22 23 31 26 68 58 16 16 36 21 11 16 22 11 56 99

139

61 24 27 31 19 30 54 37 66 62 10 11 41 38 11 17 11 11 64 99

140

80 26 28 36 16 50 87 54 75 75 33 33 16 18 12 73 96

141

52 28 25 34 16 33 35 28 58 68 34 24 8 12 22 60 96

142

35 10 9 20 23 53 96

43 31 16 33 24 20 27 33 64 55 -

143

283 142 132 169 120 130 227 200 347 313 61 50 199 151 52 84 105 73 270 340 95

144

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x IO+ Ref.

Amino

64 24 26 33 20 35 54 43 66 62 8 6 38 32 13 21 6 14 62 100

145

49 20 28 31 20 30 33 35 63 60 14 9 40 21 8 11 23 14 58 100

146

39 22 18 28 25 11 25 29 60 51 12 5 32 16 9 17 23 3 48 100

147

420= 101

215 190 240 334 178 183 285 248 344 379 46 59 145 165 145 143 111 67 -1

148

28 19 15 14 7 11 13 10 20 22 7 3 7 8 2 6 11 3 27 102

149

32 21 16 17 9 12 17 10 21 25 9 3 8 I 2 5 14 6 -1 25 103

152

index

31 21 18 16 I 10 15 9 21 24 10 3 8 13 3 6 11 7 -1 25 103

per molecular

151

31 21 17 15 8 11 17 9 20 26 8 5 6 9 1 6 15 -6 25 103

Residues

150

Protein

31 21 18 16 7 10 15 9 22 24 10 3 8 12 3 6 12 7 -1 25 103

weight

153

numbers

31 21 19 16 I 10 15 8 21 25 9 3 8 13 3 5 12 7 -1 2.5 103 12 -75 -75

-75

I55

8 6 -75 -75 -7.5 -75 -75 1 9 6 -15 2 -75 4 -75 16 104

of protein

154

2 -76 -76 -76 16 104

1 -76 -76 -16

6 -76 -76 -76 -‘6 -76

-‘6 12 -76 -76 -16

156

28 20 18 15 7 11 14 8 17 25 8 5 5 10 1 5 15 6 251 25 105

157

5 9 4 5 5 1 6 6 13 11 0 2 5 4 1 2 1 0 146 8.6 106

158

107

19 39 14 29 22 2 24 18 49 41 0 8 15 14 4 5 1 0 -77 -

159

29 46 29 36 23 1 32 29 56 42 0 2 30 14 0 8 4 _ 40 108

160

911 OP 109 0 6 9 I 01 oaf1 Z 0 IV 19 Pp LZ P 61 Of 9z 9P Pf

SLI

911 OP 165 0 8 9 Z II OSPI f 0 6fi 65 ZV 82 8 6t 8Z SZ 8P 6Z

9LI

LZ P 61

ff sz

8P

ff

82 S 61

Zf sz

SP

Zf

ELI

EP

PP

PLI

6f

09

8f

09

911 OP ILS 0 6 9 I 01 BEI Z 0

911 OP 1 19 0 6 S Z 01 PZ Z 0

ZLI

Pf

LP

Zf sz

LZ f 61

EP

09

6f

911 OP 119 0 01 9 I 01 ESPI Z 0

sz P 61

Of PZ 85

ff

fZ S OZ

Of sz LS

Zf

ff

sz LS

65

61

EZ P

19 OP

Z 0 8f

911 28Ob 165 0 6 9 I II ISPI

EP

If 8S

ff

f 81 If Iz 09

9 OZ

8f

PZ

P9 OP

Z 0 IP

PI1 OV 0 6 9 I II OSPI

Pf

LL PS

Z LP

SIT 6t7 I-01 L I El 6Z

ff

P 81 If IZ 09

PZ

P9 IP

osf1 Z 0 Ot’

PI1 OP 0 6 S I 01

IL1

OLI 891

L91

waqumu xapu! u!alo.td

691

991

u!alold 30 @!aM reln3alour lad sanptsaa

19 IP

Z 0 6f

f 0 6f 19 OP

911 OP rLS 0 6 9 1 01 PZ

911 OP 19s 0 6 9 I 11 PZ

591

LZ

P OZ 9Z 87. SP

Of

89 Pf

Z 0 Lf

El1 OP 0 9 6 0 01 @LPI

WI

LZ

P OZ 9Z 8Z t4’

Of

L9 Pf

f 0 Lf

ZII OP 0 9 8 0 01 UPI

f91

SE

III OP rss 0 P 01 I 81 SI S 0 OP 8P Pf Vf Z IZ 82. zz 8S

Z91

9z 8f 9z

ff Of PZ Zf

IP IL

ST 82 Z -

S 01 -

011 IP -

I91

If I zz Zf 62 8E Of

Of

IP f9

8LZI zz Z -

6f I IS f 8 -

601

p!X OU!uIV

au!malosI ayna3 aura au!uvfy aupt[~

Xl!lO.ld

au!uoalqL auuas

~132qmdsv

e~uoLuLue ap!tuy ueqdo~dhr~ au!solLQ au~ue@@laqd au!P!ls!H au!u~q? au!sr(T auruqw4 au!lS63-J@H ~9 3”usnm

3w c-01 x MW

acid

,,

*,,/

Glycjne Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginme Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x IO-” Ref.

Amino

34 52 29 29 16 6 24 46 59 41 0 4 17 12 2 6 8 0 55l 40 116

177

32 50 23 32 21 6 28 45 58 38 0 2 14x0 10 1 6 8 0 56r 40 116

178

33 54 25 30 19 6 28 41 57 39 0 3 1580 10 2 6 9 0 60’ 40 116

179

32 52 28 27 19 6 28 41 56 38 0 2 1580 IO I 6 II 0 57’ 40 116

180

29 46 29 27 23 3 32 35 64 36 0 2 1584 10 0 9 6 0 64 40’ 116

181

27 45 26 27 22 4 32 36 67 37 0 2 138” 10 0 8 6 0 61 40’ 116

,,

183

184

index

8,

14 6 10 8 15 4 8 5 17 21 3 5 10 2 0 5 3 4 16 117

per molecular

30 44 27 26 22 3 33 38 63 36 0 2 1386 9 0 10 7 0 62 401 116

Residues

182

Protein

19 12 11 13 13 3 12 8 28 26 1 1 9 2 0 9 8 6 21 118

weight

185

numbers

17 14 15 12 5 4 14 4 18 19 1 4 to 2 0 3 2 4 1.5 119

187

25 24 13 18 8 5 12 12 27 24 5 I 10 4 4 4 6 4 -’ 22 120

of protein

186

-87 15 16 14 5 6 8 9 17 18 5 2 8 3 0 3 5 1 121

188

19 18 10 13 9 4 7 6 20 17 5 0 4 6 1 6 5 -88 121

189

I

122

-

-1

-94

-93

18 17 9 0 5 5 1 Y2

-91

12 8 3 7

15 -90

-89

190

3 5 4

I 6 5

123

6 -6 124

-95 3 1 7 3

I6 4 1 4 7

2 -9

II 11 5 10 9 3 4 6 45

192

18 17 9 12 9 3 8 7 19

191

3 c e

z 0 G

8

E

5

$

b E;

0

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine A&tine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x lo-3 Ref.

Amino

125

696

14 18 13 7 5 5 7 8 15 17 2 5 9 2 0 4 2 4

193

28 20 15 22 10 7 11 16 25 16 2 2 9 8 1 6 9 3 w-1 23 126

194

19 15 6 12 12 4 4 8 22 25 2 1 5 4 1 9 7 3 83

195

23 127

21 15 10 20 6 5 15 8 21 23 1 1 13 6 0 13 5 4 -

196

87 144 72 97 16 56 37 42 48 59 6 14 11 69 56 24 13 11 -J 100 128

198

51 63 38 53 31 19 16 27 69 45 6 11 47 16 11 19 9 2 60 129

Residues

197

199

index

30 22 11 25 19 5 20 14 25 24 6 5 37 24 6 11 10 1 35 130

166 64 67 73 57 43 78 28 98 216 210 14 65 30 12 25 36 0 131

weight

200

numbers

2 (Continued)

per molecular

Protein

TABLE

202

119 128 116 125 64 60 73 78 118 130 17 31 95 48 12 37 65 0 -1 142 132

105 109 93 93 62 52 78 62 162 79 20 29 125 32 14 40 39 -1 127 133

of protein

201

96 103 101 101 67 50 69 65 103 93 19 28 86 36 20 35 40 -1 130 134

203

105 111 97 104 71 61 67 72 133 100 22 29 96 48 14 38 53 47 -1 130 135

204

216 136

-99

146 120 130 160 58 138 124 100 184 204 10 34 110 70 56 90 80 -

205

194 137

143 200 131 147 97 80 92 100 177 174 12 62 129 54 54 63 40 8 -1

206

’ Values for amino acids corrected for destruction during hydrolysis by using several different hydrolysis times and averaging or extrapolating to zero time. ’ Not determined. 3 Glucosamine present to the extent of 8 residues per molecule. I There may be more than 1 residue of l/2-cystine. Traces of glucosamine and galactosamine were found. The values given were calculated on the basis of 1 residue each of methionine. histidine, and arginine. 5 Number of amino acids from sequence and crystallographic results. There are 18 asparagine residues and 15 glutamine residues. Analytical results also reported. 6 Data from one hydrolysis at one fixed time and may or may not be corrected for hydrolytic destruction of amino acids. ’ Nine residues of hydroxyproline. 8 Analytical data based on 26 moles of glycine. 9 From sequence analysis. ‘O Analytical data based on 3 residues of histidine. I1 Analytical data normalized to give best over-all fit with aspartic acid, glutamic acid, glycine. and alanine. I2 Molecular weight is based on 3 residues of tryptophan per mole of protein. I3 As cystine. I4 Data from sequence. Amide ammonia distributed as 4 asparagine residues and 4 glutamine residues. I5 Data from sequence. Amide ammonia distributed as 3 asparagine residues and 4 glutamine residues. I6 One hexose residue and 2 copper atoms. I’ Two atoms copper. ISTwo atoms each of copper and zinc. Is Minimum number of residues calculated assuming one residue each of histidine and tyrosine. 2o Values given based on 22 residues of arginine per subunit. a1The number of residues per mole was determined by assuming 24 glycine and 18 lysine residues. There are 3 cysteine residues. ?* There are no free sulfydryl groups. The carbohydrate content is 26% and consists of 33 residues of hexose, 16 residues of N-acetylhexosamine and 16 residues of N-acetylneuraminic acid, all per 55,000 daltons. *3 The molecular weight of the polypeptide chain is 49,000 and it corresponds to a glycoprotein of 54,000. Factor X, has 3 mannose and 6 galactose residues. 24The molecular weight of the polypeptide chain is 49.000 and it corresponds to a glycoprotein of 54.000. Factor X, has 4 mannose and 6-7 galactose residues.

E

2 K =

2

z

2 m ul 0 a

25There is approximately 10% carbohydrate which consists of 10 residues hexose (galactose and mannose), 10 residues hexosamine (glucosamine and galactosamine calculated as residues of IV-acetyl hexosamine) and 7 residues of neuraminic acid (includes N-acetyl and N-glycolyl derivatives calculated as N-acetylneuraminic acid). 26 There is approximately 10% carbohydrate which consists of 9 residues hexose, 10 residues hexosamine, and 7 residues of neuraminic acid, alJ calculated as described in footnote 25. w Trace. 28The carbohydrate content, all on heavy chain, is: 8 moles hexose, 8 moles sialic acid, and 6-7 moles hexosamine. *9 The carbohydrate content, all on heavy chain, is: 10 moles hexose, 9-10 moles sialic acid, and 7-8 moles hexosamine. 3o There is approximately 12% carbohydrate consisting of 8 residues hexose, 6 residues hexosamine, and 5 residues neuraminic acid calculated as described in footnote 25. 31There is approximately 2% carbohydrate consisting of 1 residue of hexose with small amounts of hexosamine and neuraminic acid calculated as described in footnote 25. 32There is approximately 11% carbohydrate consisting of 8 residues hexose, 7 residues hexosamine, and 5 residues neuraminic acid calculated as described in footnote 25. 33There is approximately 1% carbohydrate consisting of 1 residue of hexose and small amounts of hexosamine and neuraminic acid calculated as described in footnote 25. 34There is approximately 3% carbohydrate consisting of 3 residues hexose, 2 residues hexosamine, and a small amount of neuraminic acid, calculated as described in footnote 25. 35There is approximately 25% carbohydrate consisting of 6 residues of hexose, 4 residues hexosamine, and 3 residues neuraminic acid calculated as described in footnote 25. 36The molecular weight of 320,000 includes 5% carbohydrate. 37All exist as cystine in protein. 38The analytical data based on 6 residues of leucine. 39The analytical data based on 1 histidine and 3 glutamic acid residues per mole. Same results obtained from sequence (46). There are 3 asparagine and 1 glutamine residues (46). 4oNo detectable sulfhydryl group. 41 Analytical data corrected to 1 tryptophan residue. This analysis is for protein from 1968 seeds. Analysis of the protein from 1969 seeds is also given in Ref. 47. 42 Analytical data reported as residues per mole of vitamin B12. Carbohydrate content of approximately 8% consisting of 12 residues mannose, 3 residues galactose, 2 residues fucose, 5 residues N-acetylglucosamine, 4 residues N-acetyl galactosamine, and 4 residues N-acetylneuraminic acid. 43In Ref. 53 is also presented the analysis of intrinsic factor-vitamin B,,, a complex. The data reported in the table are of the apoprotein. M From sequence find 6 residues asparagine and 2 residues glutamine. 2

E iz g z” if

i:

2 u

8

%

d5No sulfhydryl groups detected in protein. 46The carbohydrate consists of 4 residues fucose, 8 residues mannose, 9 residues galactose, 14 residues N-acetyl glucosamine, and 2 residues N-acetylneuraminic acid. (7 There is one cystine residue and 1 asparagine residue. 48There is O-1 residue of methionine. 49There are 7-8 residues of half-cystine. 5oThere are 6-7 residues of aspartic acid. 51There are 7-8 residues glutamic acid, 7-8 residues half-cystine. and 4-5 residues glycine. 52 From sequence there are 3 asparagine and 4 glutamine residues. 53From sequence there are 2 glutamine residues. 54 From sequence there are 4 asparagine and 3 glutamine residues. 55From sequence there are 3 asparagine and 2 glutamine residues. 56 From sequence there are 1 asparagine and 2 glutamine residues. 57 From sequence there are 5 asparagine and 6 glutamine residues. 58There are 10-l 1 glutamic acid residues. 5sFrom sequence there are 4 glutamine residues. There is also sequence heterogeneity at positions 6, 12, 33, and 96: Leu/Val at 6, Pro/Ala at 12, GlulAsp at 33, and GlylAIa at 96. 60 From sequence there are 3 asparagine and 2 glutamine residues. fil There are 4-5 residues. 62There is O-l residues. 63There are 2-3 residues. 64From sequence there are 4 glutamine residues. 65From sequence there are I asparagine and 2 glutamine residues. 66There are 4-5 residues. 67 There are 7-8 residues. 68There are 8-9 residues aspartic acid and IS-16 residues of glutamic acid. 6y From sequence there are 2 asparagine and 4 glutamine residues. ‘O From sequence there are 6 glutamine residues. 71There are 118 or 129 residues histidine, 21 t 1 residue tryptophan, 570 or 620 residues leucine, 78 or 92 residues isoleucine, 212 or 180 residues of serine. 72 or 56 residues proline, 48 + 2 residues I/2-cystine, and 67 or 74 residues methionine. 72Carbohydrate content in % by weight: sialic acid. 8.50; galactose, 4.50: mannose, 3.00: glucosamine as N-acetylglucosamine, 6.75; galactosamine. 6.75%. K cn

2 2 E z v) < z

G

B

s $*

b 6

0

73MW of 323,000 is the weight of the protein moiety. It was calculated by subtracting 5%, for carbohydrate content, from the weight of fibrinogen. In ref. 97 there are the amino acid analyses of other anticoagulant derivatives of fibrinogen. 74 Assumes 5% of molecular weight contributed by carbohydrate and lipid. 75 Aspartic acid, 16-18 residues; threonine, lo-11 residues; serine, 1l-12 residues; glutamic acid, 14-17 residues; glycine, 15-16 residues; valine, 12-13 residues; I/2-cystine, 3-4 residues; leucine, 7-8 residues; histidine, l-2 residues; tyrosine, 7-8 residues (by column), 6-7 residues (spectrophotometrically); amide NH,, 13-14 or 18-19 residues. ‘6 Aspartic acid, 16-17 residues; threonine, 9-10 residues; serine, 9-12 residues; glutamic acid, 15-16 residues; glycine, 15-16 residues; valine, 12-14 residues; l/2-cystine, 3-4 residues; isoleucine, 8-9 residues; leucine, 7-8 residues; lysine, 9-10 residues: histidine, l-2 residues; arginine, 6-7 residues; tyrosine, 7-8 residues (by column), 6-7 residues (spectrophotometrically): tryptophan, 3-4 residues; amide NH,, 17-25 residues. ” Data from sequence. ‘* Results calculated on basis of 12 residues of arginine. 79 Plus 12 residues eN-methyllysine. 8oPlus 9 residues e--N-methyllysine. 8* Plus 11 residues of eiV-methyllysine. 82 Amino acid analysis of another 1,2 flagellin of this same organism reported in ref. 116. 83Plus 10 residues of e-IV-methyllysine. *4 Plus 13 residues of e--N-methyllysine. 85 Plus 15 residues of eN-methyllysine. 86 Plus 16 residues of E-N-methyllysine. 87 There are 14-15 residues of glycine. ** There are l-2 residues of tryptophan. *9 There are 16-17 residues of glycine. 90 There are 9-10 residues of valine. 91 There are 6-7 residues of threonine. 92Ammo acid analysis based on 1 mole of histidine. 93There are 5-6 residues of phenylalanine. 94There are 4-5 residues of tyrosine. 95There are 13-14 residues of aspartic acid and 16-17 residues of glutamic acid. 96From sequence there are 5 residues of asparagine and 1 residue of glutamine. In ref. 125. may also be found the results of amino acid analyses of an hydrolyzate of the protein. 97There is O-l residue of tryptophan. OSFucose, 3.4 residues; mannose, 30 residues; galactose, 10 residues; glucosamine, 12 residues (based on 90% recovery); galactosamine, trace.

AMINO

ACID

ANALYSES

OF

PROTEINS

VII

147

REFERENCES 1. 2. 3. 4.

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