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A compilation of amino acid analyses of proteins. III
ANALYTICAL
BIOCHEMISTRY
A Compilation
52, 234-264
of Amino DONALD
Department
of Biochemistry,
Received
(1973)
Acid
Analyses
of Proteins.
III
M. KIRSCHENBAUM
College of Medicine, Downstate Brooklyn, New York 11205
September
8, 1972;
accepted
October
Medical
Center,
10, 1972
In this paper, the third of the series (1,2), I have added an additional 173 proteins for which amino acid analyses have been published. The molecular weights have been rounded off to the nearest hundred for weights under 10,000 and to the nearest thousand for weights above 10,000. The number of residues have been rounded off to the nearest integral number. Methods of analysis are those described previously (1,2), and occasionally cysteine was determined using the dimethyl sulfoxide procedure (3) or by reaction with 2-bromoacetamido-4-nitrophenol (4). Table 1 is the Protein Index and gives the names of the proteins, the enzyme commission numbers supplied by the references cited, and the sources of the proteins. Table 2 gives the amino acid analysis, amide ammonia, molecular weight, and literature citat,ion. Aspartic acid includes asparagine residues converted to aspartic acid during hydrolysis. Glutamic acid includes glutamine residues converted to glutamic acid during hydrolysis. TABLE Number 1.
2a. 2b. 2c. 3.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
Aldolsse, fructose 1,6diphosphate Mustelus canis (shark) Aldolase A, EC 4.1.2.7 Human muscle Aldolase B, EC 4.1.2.7 Human liver Aldolase C, EC 4.1.2.7 Human brain Allantoicase, 30% 0.9s + 70% 10.85 Pseudomonas aeruginosa (a bacterium)
Copyright
@ 1973 by
All
of
riehts
1: Protein
rmvm+~rtinn
Academic in
Press, REV
fnrm
Index 4.
Name:
5.
Source: Name:
6a.
Source: Name:
6b.
Source: Name: Source:
7.
234 Inc. r~=~=rv~d
Name:
n-Amino acid oxidase, EC 1.4.3.3 Pig kidney &Aminolevulinate dehydratase, EC 4.2.1.24 Mouse liver or-Amylase (IEP = 8.95), EC 3.2.1.1 Rat pancreas cY-Amylase (IEP = 8.77), EC 3.2.1.1 Rat pancreas Anthranilate wynthetase: anthranilate 5-PRPP
AMINO
ACID
ANALYSES
TABLE
Source:
8. Name: Source: 9. Name: Source: 10. Name: Source: 11. Name: Source: 12a. Name: 12b.
Source: Name:
13.
Source: Name:
Source: 14. Name: Source: 15a. Name: Source: 15b.
16.
Name: Source: Name:
Source:
phosphoribosyltransferase Salmonella typhimurium (a bacterium) Antibody, anti-human blood group H(0) Anguilla rostrata (eel) Apoferritin Horse spleen Apoprotein, C&-isoprenoid alcohol phosphokinase Staphylococcus aureus membrane Arginase, EC 3.5.3.1 Rat liver Argininosuccinase, EC 4.3.2.1 Bovine kidney Argininosuccinase, EC 4.3.2.1 Bovine liver Arylsulfatase A, monomer Human urine Ascorbic acid oxidase Corcubita pepo condensa (yellow crookneck squash) Aspergillopeptidase A Aspergillus
satoi
(a common mold) Aspergillopeptidase Aspergillus
A
satoi
OF
PROTEINS.
1 (Continued) 19b.
Name:
19~.
Xame:
20a.
Source: Name:
Source:
Source: 20b.
Name: Source:
21a. Name: Source:
Zlb.
Name: Source: 21~. Name: Source: 22. Name: Source: 23.
Name: Source:
24a.
Name: Source: 24b. LVame: Source: 24~. Name: Source: 24d. Name: Source: 25. Name: Source..
(a common mold) Bacteriophyll-protein complex
26.
Name: Source:
Chloropseucbmonas ethylicum (a bacterium)
27.
Name:
17. Nqe: Bacteriocm DF13 Source: Enterobacter cloacae (a bacterium) 18. Name: Bacteriophage +x174, protein Source: Bacteriophage 4x174 19a. Name: Bacteriophage 6x174 particle Source: Bacteriophage 6x174
235
III
28.
29.
Bacteriophage subunit o Bacteriophage Bacteriophage subunit p Bacteriophage Bacteriophage particle Bacteriophage Bacteriophage subunit B Bacteriophage Bacteriophage Bacteriophage Bacteriophage Bacteriophage Bacteriophage Bacteriophage Bacteriophage protein Bact.eriophage Ch Human serum
+x174, +x174 9x174, +x174 S13 S13 S13, S13 h ghosts h X heads X x tails x xf coat xf
c3
Human serum C3a (C4,2) Human serum C3a(Try) Human serum C3a(NH20H) Human serum Calliphorin Calliphora erythrocephala (blowfly) Calsequestrin Rabbit sarcoplasmic reticulum Carbamate kinase, EC 2.7.2.2
Source:
Streptococcus
Name:
(a bacterium) Carbamyl phosphate synthetase
faecalis
Source:
Escherichia
Name: Source:
(a bacterium) Carbonic anhydrase X, Human erythrocyt,es
coli
236
DONALD
M.
TABLE 30. 31. 32. 33. 34.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
35a. 35b. 36.
Name: Source: Name: Source: Name: Source:
37. 38. 39. 4th
Name: Source: Name: Source: Name: Source: Name: Source:
40b.
Name:
44a.
Source: Name: Source: Name: Source: Name: Source: Name:
44b.
Source: Name:
45a.
Source: Name:
45b.
Source: Name:
45~.
Source: Name:
41. 42. 43.
Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Bovine erythrocytes Carbonic anhydrsse low activity Bovine rumen Carbonic anhydrase low activity Bovine rumen Carbonic anhydrase Deer erythrocytes Carbonic anhydrase Goat erythrocytes Carbonic anhydrase Sheep erythrocytes Carbonic anhydrase, major component Sheep erythrocytes Carbonic anhydrase, minor component Sheep erythrocytes Carbonic anhydrase, low activity Guinea pig erythrocytes Carbonic anhydrase, high activity Guinea pig erythrocytes Carbonic anhydrase,
KIRSCHENBAUM 1 (Continued)
Y A 46a.
Source: Name:
B Source: B 46b.
Name:
B Source: B 47. B 48a. C 48b. C 49. C B
50.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
a, 51a.
Name:
51b.
Source: Name:
51~.
Source: Name:
51d.
Source: Name:
52.
Source: Name:
b,
C C
C
SOUTCe:
53a. 53b.
Name: Source: Name:
53~.
Source: Name:
54a.
Source: Name: Source:
secondary high activity isozyme Guinea pig erythrocytes Carbonic anhydrase, low activity Guinea pig colonic mucosa Carbonic anhydrase, high activity Guinea pig colonic mucosa Carbonic anhydrase Guinea pig stomach Carbonic anhydrase B Macacu mu&a (monkey) Carbonic anhydrase C Macuca mulata (monkey) Carbonic anhydrase Galwcerclo cuvieri (tiger shark) Carbonic anhydrase Carcharhinus leucas (bull shark) Carboxylesterase, EC 3.1.1.1 Pig liver Carboxylestersse EC 3.1.1.1 Pig liver Carboxylesterase EC 3.1.1.1 Pig kidney Carboxylesterase EC 3.1.1.1 Pig kidney Carboxylesterase EC 3.1.1.1 Bovine liver Carboxypeptidase BI Bovine pancreatic juice Carboxypeptidase BI, heavy chain Bovine pancreatic juice Carboxypeptidase BI, light chain Bovine pancreatic juice Carboxypeptidase BII Bovine pancreatic juice
AMINO
ACID
ANALYSES
TABLE 54b.
Name:
54c.
Source: Name:
55. 56. 57. 58a. 58b. 58~. 59a. 59b. 60. 61. 62a. 62b. 63a. 63b. 64. 65. 66. 67a. 67b.
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: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name:
Source: 68a. Name: Source:
Carboxypeptidase heavy chain Bovine pancreatic Carboxypeptidase light chain Bovine pancreatic Carboxypeptidase Bovine Carboxypeptidase Squalus acunthias Pacific dogfish) cd2asein A Bovine milk oc.$&sein B Bovine milk orJ1-Casein B Bovine milk or,&asein B Bovine milk cy,&!asein C Bovine milk c.&&sein C Bovine milk ol,l-Casein BC Bovine milk ~&asein D Bovine milk a,,&asein Bovine milk aB,&asein Bovine milk a..&asein Bovine milk or,,r-Casein Bovine milk cr,,.&asein Bovine milk @-Casein Bovine milk @-Casein A Bovine milk j%Casein A1 Bovine milk @Casein A1 (HissAspoGlua) Bovine milk &Ca.sein A* Bovine milk
OF
PROTEINS.
III
1 (Continued)
BII,
68b.
Name:
juice BII,
68~.
Name:
juice B
68d.
Name:
B (spiny
69a.
Source:
Source:
Source:
69c.
70a. 70b. 7oc. 71a. 71b. 71c. 71d.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
72. Name: Source: 73. Name: Source: 74. Name: Source: 75. Name: Source: 76. Name: Source: 77. Name: Source: 78a. Name: Source: 78b. Name: Source:
@-Casein AZ-1 (His&p,~Glu& Bovine milk p-Casein Azde (Hisdsp~~Glud Bovine milk @%.sein AZ+ (H~wQJPQG~u~~) Bovine milk @-Casein B Bovine milk &Cssein B Bovine milk &Casein B Bovine milk p-Casein B-l Bovine milk fMa.sein B-2 Bovine milk B-Casein B. Bovine milk p-Casein C Bovine milk p-Casein C Bovine milk @Casein C Bovine milk fi-Casein C Bovine milk (Abondance cow Simmental type) p-Casein D Bovine milk r-Casein A2 Bovine milk &asein B Bovine milk K-Casein Bovine milk K-Casein Bovine milk K-Casein A Bovine milk K-Casein A-l Bovine milk &&sein A-2 Bovine milk
237
238
DONALD
M.
TABLE 78~. 79. 80a. 80b. 81. 82a. 82b. 82~. 83a. 83b. 83~. 84. 85. 86. 87. 88a.
88b. 88~. 88d. 88e. 89a.
89b.
&asein A-4 Name: source: Bovine milk Name: K-Casein B Bovine milk Source: Name: K-Casein B-l Bovine milk Source: Name: dhsein B-2 Bovine milk Source: Name: para-&asein Source: Bovine milk para-K-c&S& A (0.60) Name: Source: Bovine milk para-r-Casein A Name: Source : Bovine milk Name: paTa-K-CaSein A Bovine milk Source: Name: para-r-Casein B (0.52) Source: Bovine milk Name: para-r-Casein B Bovine milk Source: Name: pa?U-K-&S& B Source: Bovine milk Catalase Name: Source: Bovine liver Name: Catalase Source: Horse liver Name: Catalase Source: Rat liver Name: Cellulase Source: Myrothecium verrucaria Ceruloplasmin I Name: (Cohn IVa) Human plasma Source: Name: Ceruloplasmin IIa Source: Human plasma Ceruloplasmin IIb Name: Human plasma Source: Name: Ceruloplasmin IIIb Source: Human plasma Name: Ceruloplasmin Source: Human plasma Ceruloplasmin, Name: component I Source: Pig serum Name: Ceruloplasmin, component II Source: Pig serum
KIRSCHENBAUM 1 (Continued) 9Oa. 90b. 91. 92.
Name: Source: Name: Source: Name: Source: Name: Source:
93.
Name:
94.
Source: Name: Source:
95a.
Name:
Source: 95b.
Name:
Source: 95c.
Name:
Source: 96.
97. 98. 99a. 99b. 100. 101. 102.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
Ceruloplasmin I Albino rat Ceruloplasmin II Albino rat Chloroperoxidase Calduriomyces fumago Chlorophyll a-Protein Beta vulgaris (spinach beet) chloroplasts Chloroplast coupling factor; CF, Spinach chloroplasts Chloroplast fraction I protein Beta vulgaris (spinach beets) chloroplasts Chorismate mutaseprephenate dehydrogenase Aerobacter aerogenes (a bacterium) Chorismate mutaseprephenate dehydrogenase Aerobacter agogenes (a bacterium) Chorismate mutaseprephenate dehydrogenase Escherichia wli (a bacterium) Chromaffin granule protein Bovine adrenal medulla Chymopapain B Papaya Chymosin Calf stomach Chymotrypsin C. Pig pancreas Chymotrypsin C Pig pancreas Chymotrypsin II Human pancreas Chymotrypsin Chicken pancreas Chymotrypainogen Rat pancreas
AMINO
ACID
ANALYSES
TABLE 103~~. Name: Source: 103b. Name: Source: 103~. Name: Source: 103d. Name: Source: 104. Name: Source: 105a.
Name: Source:
Chymotrypsinogen A Pig pancreas Chymotrypsinogen B Pig pancreas Chymotrypsinogen C Pig pancreas Chymotrypsinogen C Pig pancreas Chymotrypsinogen Squalus acunthias (spiny Pacific dogfish) Chymotrypsinogen A Bovine pancreas
OF
PROTEINS.
III
239
1 (Continued) 105b.
Name: Source: 106a. Name: Source: 106b. Name: source:
106~. Name: Source: 107a. Name: Source: 107b.
Name: Source:
Chymotrypsinogen A Bovine pancreas Chymotrypsinogen B Bovine pancreas Chymotrypsinogen B Bovine pancreas Chymotrypsinogen B Bovine pancreas Cocoonase Anthe-raea pernyi (Chinese oak silk moth) Cocoonase Antheraea polyphemus
8. 9. 10. 11. 12a. 12b. 13. 14.
6a. 6b. 7.
5.
1. 2a. 2b. 2~. 3. 4.
acid
Aldolase Aldolase A Aldolase B Aldolase C Allantoicase ~-Amino acid oxidase &Aminolevulinate dehydratase a-Amylase a-Amy&e Anthranilate synthetase Antibody Apoferritin Apoprotein Arginase Argininosuccinsse Argininosuccinsse Arylsulfatase A Ascorbic acid oxidase
Amino
92 10 9 90 124 121 124 94
51 52 170
22
124 130 117 129 10 43
A Compilation
89 14 14 64 156 151 62 76
35 35 274
29
1 35
173 186 180 181
29
108 156 147 135 8 47
66 55 725 11 23 86 71 102 209 98 202 50 50 79 91
35 24 36 23 135 254
6
78 74 79 91 8 34
of Amino
Acid
12
58 42 3 3 23 4 51 71 60 62 59 61 25 149 72 92
24 21 23 20 85 106
7
90 74 83 113 77 90 73 104 4 5 19 16
Analyses
74 9 8 60 141 139 74 73
33 35 131
14
67 86 79 75 5 17
74 5 8 68 96 96 37 70
24 24 123
14
116 83 65 72 5 29
110 17 8 87 143 138 74 132
86 81 232
17
107 102 111 117 10 34
TABLE of Proteins
90 24 8 87 199 191 112 100
32 34 251
31
154 170 177 165 10 45
46 3 0 7 17 16 18
10 10 53
28
32 -a 1 16
2 (in residues
6 3 4 13 53 51 12 17
10 11 61
7
6
27 16 27 15 a
31 9 8 87 73 76 50 55
27 26 72
12
109 142 128 109 5 19
per molecular
13 13 65
6
43 38 40 28 2 12
53 38 9675 53104 33 23 110 45 116 47 37 39 37 39
28 26 137
14
51 69 65 83 4 28
weight
29
24 36 36 12 50
31 52 51 25 53
16 16 57
8
47 54 41 47 2 15
18
26 25 68
12
44 35 42 39 4 17
of protein)
8 181
6 -
12 110 310 35
10 130 2-19 412 35 35 50 -
-
-
17 118 190 188 110 -6
1236
56 56 280
40
160 160 160 160 113 504
8 9 10 11 12 12 13 14
67
6
5
4
22 2 3
1
ii
F w i;i :: X g t?
5
8
23. 24a. 24b. 24~.
22.
21~.
21b.
21a.
2Ob.
20a.
19c.
19b.
19a.
16. 17. 18.
15b.
15a.
Aspergillopeptidase A Aspergillopeptidase A Bacteriophyll Bacteriocin DF13 Bacteriophage 4x174 protein Bacteriophase 6x174 particle Bacteriophage 4x174 subunit Bacteriophage 4x174 subunit Bacteriophage S13 particle Bacteriophage 513 subunit Bacteriophage ?a ghosts Bacteriophage A heads Bacteriophage X tails Bacteriophage xf coat protein Clq C3 C3a(C+ 2) C3a(Try)
580 93 3 3
9
33
20
15
16
18
15
14
16
34 71 17
31
32
148 87 3 3
6
38
25
18
15
15
15
15
16
21
11
16
17
16
17
16
18 29 18
19
20
185 201 129 132 25 34
81
38
25
14
12
13
12
21
14
29 30 14
18 50 15
15
22
22
20
20
19
16
8
16
14
13
16
13
15 39 15
10
10
2
29
20
13
14
15
12
18
14
23 35 15
42
43
I2
40
19
15
14
16
16
17
16
13 25 17
25
25
34
33
18
29
26
23
25
23
33 56 27
34
35
128 20213 18515 17715 285 64 73 94 92 143 13 3 3 4 23 3 3 5
31
10
11
6
9
10
10
8
10
20 16 10
11
12
308 204 6 6
I
30
40
20
17
17
19
14
17
28 54 18
22
22
7
10
5
19
6
6
10
3 7 5
0
0
82 85 34 26 42 42
02
1
1
1
l-
11
1
9
2
2 0 2’
1
1
2
12
18
9
11697--
12
001
1
1
1
6
6
4
512
10
12
6
12
10
13
15 12 11
13
13
7
12
6
9
6
2
Y--
8 12 10
17
18
12314 144 47 142 1O1’6 100 63 25 54 51 5 s121-5 7121--
2
18
17
10
11
10
11
7
9 9
11
7 10 5
3
1 18 23 12
3
1
9
16 51 9
11
11
-
-
-
l-
4 -
2 -
I -
30 -
-
-
-
31
32
4.9
36
34
19
8
*
s
*
*
33 56 26
35
36
23 24 24 24
22
21
21
21
20
20
19
19
19
16 17 18
15
15
continued
388 185 7.2 7.2 Table
5 7 8 6 -
I
1
36.
35b.
35a.
34.
33.
32.
31.
30.
29.
24d. 25. 26. 27. 28.
acid
C3a(NH20H) Calliphorin Calsequestrin Carbamate kinase Carbamyl phosphate synthetase Carbonic anhydrase X, Carbonic anhydrase Y Carbonic anhydrase A Carbonic anhydrase B Carbonic anhydrase B Carbonic anhydrase B Carbonic anhydrase B Carbonic anhydrase B Carbonic anhydrase C
Ammo
22
162”
16
15
16
16
17
24
15
6 193 15 28 148
13
19
19
18
19
20
20
14
19
3 117 26 35 195
17
17
18
17
17
17
17
16
27
20
21
19
20
20
20
29
us 20
36 213 209 27 35 27 27 134 143
9
9
10
10
10
10
10
9
8
18
17
18
15
18
18
18
16
17
22 143 110 20 20 22 16 109 76
19
30
30
27
30
30
30
19
29
4 154 14 14 80
TABLE
13
14
14
13
14
15
15
12
m
29
31
31
31
31
32
31
r’
30
3 5 172r6 426 11 74 16 31 107 182
24
22
22
22
24
25
24
26
22
7-361 72 43 225
2 (Continued)
1
1
1
1
1
1
1
1
1
I
2
2
2
2
2
2
1
2
18 162 3 6 3 6 21 45
25
18
18
18
18
19
19
27
17
5 295 26 24 96
7
7
7
7
7
7
7
8
8
12
11
11
11
11
11
11
lo
11
13
11
11
10
11
11
11
13
IO
9
8
8
8
8
8
8
9
21
9221-116 118 400 442 7 6 24 6 3 6 6 5 LO2 36 71 54
7
6
6
6
6
6
7
7
6
21
26
27
25
272’
27
27
23
za
64 2 34 15 -
3027
29”
3027
2827
30
30
30
32
29
7.8 530 44 31 200
33
33
33
32
31
30
30
29
29
24 25 26 27 28
37. Carbonic anhydrase 38. Carbonic anhydrase 39. Carbonic anhydrase 40a. Carbonic anhydrase 40b. Carbonic anhydrase 41. Carbonic anhydrase 42. Carbonic anhydrase 43. Carbonic anhydrase 44a. Carbonic anhydraae 44b. Carbonic anhydraee 45a. Carbonic anhydrase 45b. Carbonic anhydrase 45~. Carbonic anhydrase 46a. Carbonic anhydrase 46b. Carbonic anhydrase
C
C
C
b
a
B
C
C
20
20
1731
1932
19
17
19
18
18
20
19
19
20
19
24
20
2299
22y9
17
13
13
18
18
21
21
18
18
20
22
22
17
18
18
18
18
22
22
23
23
22
15
16
20
17
17
25
20
24
25
20
26
26
28
28
26
25
25
26
26
25
8
11
8
8
11
3
3
3
5
2
10
10
5
9
9
17
16
17
17
16
23
20
21
21
21
20
20
20
17
17
21
33
24
22
33
15
18
18
18
17
26
26
16
17
19
11
11
12
12
11
9
11
13
12
13
10
10
15
12
13
25
25
25
25
25
32
33
32
32
32
30
30
32
29
29
25
24
25
25
23
24
25
27
26
23
21
22
24
25
27
-
-
-
-
-
1
1
0
0
0
0
1
0
1
1
3
0
3
3
1
330
3='
3
33"
2
1
1
3
1
1
23
19
23
23
19
18
18
19
20
20
20
21
19
24
24
11
11
12
12
13
11
10
11
12
12
5
5
14
5
14
10
6
14
51098
9
10
10
10
11
7
8
9
7
7
11
9
11
11
12
12
12
13
13
11
11
11
12
12
7
8
7
7
6
7
7
7
7
7
7
8
8
8
-
-
-
-
-
-
-
-
-
7 -
6-
-
6 -
6 -
5 -
5 -
7-
7
7
7
Table
2628
21
2196
-
37
37
37
37
37
36
36
35
35
35
34
34
31
30
31
wntinued
28
30
29
28
30
30
-
-
-
30
30
3P'
30
3op1
acid
47. Carbonic anhydrase 48a. Carbonic anhydrase B 48b. Carbonic anhydrase C 49. Carbonic anhydrase 50. Carbonic anhydrase 51a. Carboxylesterase 51b. Carboxylesterase 51~. Carboxylesterase 51d. Carboxylesterase 52. Carboxylesterase 53a. Carboxypeptidase BI 53b. Carboxypeptidase BI 53~. Carboxypeptidase BI 54a. Carboxypeptidsse BII
Amide
19
16
12
23
19
110 109 92 107 115 24
17
7
23
19
15
22
32
30
116 123 107 126 101 23
17
7
22
15
5
10
117 120 95 111 109 16
10
13
14
16
17
21
5
16
143 142 119 139 152 21
32
32
24
19
25
8
15
12
647879214
9
28
21
85 99 28
29
53 98 58 103 15 13
24
12
31
78 SO 73
21
16
30 18
24
49 107 45102 46 84
17 16
18
10 10
8
TABLE
28
20
72 67 28
74 71 61
11
13
13 11
12
28
23
126 129 30
128 120 108
33
40
36 30
25
27
17
144 127 26
155 151 124
41
40
22 26
25
2 (Continued)
-
8
5
10 11 8
17 14 9
25
18
1 1
6
4
31 26 5
25 30 26
2
3
1 2
3
17
14
91 89 17
92 89 78
26
29
18 24
23
12
6
2
4
8
35 32 29
9
14
34 40 5
3
12
13
5
7
69 71 13
71 71 59
12
18
910 12 11
15
49 47 11
45 42 42
10
13
7 8
5
20
2
16
37 34 20
35 37 31
8
9
9 7
7
3627
4027
2827 292’
30
10
4-
6 -
35
10
25
1673* 167= 35
30 18P 167 30 110S4 167 26 1583516737
5 -
7 -
77 -
-
30 185= 53 155 10 -
-
41
41
41
40 40 41
40 40 40
39
39
38 38
37
2
: w Ed 0” Di g $
i
g
E
57. %a. 58b. 5th. 59a. 59b. 60. 61. G2a. 62b. 63a. 63b. 64. 65. 66. 67a. 67b. 68a. 68b. 68~. 68d. 69a. 69b.
56.
55.
54~.
54b.
Carboxypeptidase BII heavy chain Carboxypeptidase BII light chain Carboxypeptidase B Carboxypeptidase B a,,-Casein B a,l-Casein B ol,l-Casein B ol,l-Casein B a,,-Casein C or,&asein C ol,&asein BC c&Za.sein D Ly.,3-Casein ol,,&nsein ay,,&-Caseio ru+-Casein cu,,s-Casein /%Casein &Casein A p-Casein A1 o-Casein A1 @-Casein A? &Casein AZ-l &Casein A2e2 @-Casein AZ+ @-Casein B fi-Casein B
16
10
24
22
11 10 11 11 9 9 11 11 12 I1 12 11 46 11 11 10 2 6 4 11 2 6 4 11 9 24 5 5 5 5 565 5 5 5 556 5 5 6 5 5 5 5 5 5 5 555
20
22
17
22
17
12 17 13 20 11 17 14 21 14 21 14 21 14 21 13 20 10 9 19 17 10 9 20 18 37 37 1921 20 22 18 21 19 21 18 21 19 21 18 21 18 21 20 22 18 21
17
14
7754546879214
16
14 13 11 14 13 14 14 13 8 15 7 15 29 10 10 10 9 10 10 10 9 10 10
20
15
10
21 20 17 21 20 21 21 21 8 16 7 15 30 33 64 33 34 34 35 33 36 64 33
14
13
8
25
25
19
18 7 17 6 164’ 5 6 17 18 6 17 6 6 17 6 16 10 12 20 23 10 6. 20 21 38 38 14 9 15 9 15 9 15 9 15 9 14 9 15 9 15 10 15 9 14 9
25
25
20
20
25
17
17 47 1S 46 1542 3943 19 49 18 46 19 48 19 45 18 47 13 29 26 56 12 28 25 56 52 112 9 39 9 40 9 139 9 '40 9 39 10 39 10 38 9 38 9 39 9 39
31
28
22
-
1 1’9 151 2 45'
0 0 0 0
7
5
5
18 17 14 17 17 17 17 17 15 30 16 3'2 63 11 11 11 11 11 11 11 11 11 11
6 ss2 5 9 6 6 6 6 6 6 6 6 6 6
15
17
15
6 6 5 6 6 6 6 5 3
8
6
5
8 17 4 4 4 4 4 4 4 4 5 5
6 7 6 7 7 7 7 6 4347 434-
14
13
5
6 6 5 6 6 6 6 7
4
7
5
6 10 6 6 6 6 5 5 5 5 6 6
4252
8
20
22
--
27 3 22 344' 30 3444 344' 33'7
Table
1 30s3 1 -M 1 25% 1 A5 1 2553 1 2P 1 2455a 1 2gS3 1 --XJ
4 -
7-
3 3 2 4 3 4 4 3 7-
-
8 -
4-
6-
10
914 -18 28 9 4----L39 4 9 4 9 4 9 4 9 4 9 4 9 4 9 4 9 4
814
812 10 12 8 10 10 12 10 12 10 12 10 12 10 11
9
12
716
44 44 45 46 44 46 46 47 48 49 48 49 49 50 51 52 53 52 53 53 53 51 52
44
42
41
41
continued
24 24 24 24 24 24 24 24 24
-
28 29 24 30 29 30 30 29 -48 -48
34
-4o
10
25
69c. 70a. 70b. 70~. 71a. 71b. 7lc. 71d. 72. 73. 74. 75. 76. 77. 78~ 78b. 78~. 79. 80a. 80b. 81. 82a. 82b.
acid
p-Casein B p-Casein B-l pCasein B-2 &Casein B, p-Casein C p-Casein C &Casein C &Casein C &Casein D +hsein A2 r-Casein B K-Casein dhsein &asein A t&asein A-l t&hsein A-2 &asein A-4 &asein B &h&n B-l K-Casein B-2 para-&asein para+Casein pat-a-&asein
Amino
A A
56S 5 5 5 556 555 5 5 555 5= 5= 5 3 4 3 4 3 4 3 2 2 3 4
5 5 5 6 5 7 5 5 7 6 6 18 13 20 74 14 14 21 14 14 10 14 13
.._~ --.
19 19 19 17 18 19 18 20 63 20 20 13 10 16 75 11 11 16 11 10 7 9 9
_ ~~..
6o 21 22 20 21 21 21 22 20 23 23 14 9 7o 8 8 77 7o 8 8 8 11 12
10 10 10 10 10 11 10 10 10 8 8 14 12 17 11 76 11 18 12 12 7 10 9 69
33 35 5a 33 34 34 L4 54 41 40 23 18 27 20 20 21 28 20 20 13 18 18
14 14 14 15 15 15 15 15 16 13 12 18 11 6* 73 14 11 68 73 12 8 11 10
TABLE
9 9 9 10 9 10 9 9 11 10 10 17 12 67 14 15 15 67 13 13 5 6 5
9 9 9 S6 9 10 9 9 10 9 9 17 11 17 12 16 12 16 11 11 8 11 12 27 27 18 27 27
99
38 40 40 Vi 37 62 38 39 57 39 39 36 25 69 27 27 26
2 (Continued)
-
2 2 2 2 2 2
179
179
1 2 2 2
6 6 6 5 6 6 5 6 5 7 7 2 2 3 2 2 2 3 2 2 1 1 1
11 11 11 11 12 12 12 12 12 12 12 12 9 13 9 9 9 13 9 9 7 9 9
5 5 5 5 4 4 4 4 4 3 4 7 5 8 5 5 78 8 5 5 5 8 7
6 9 6 9 6 9 6 9 6 9 6 9 6 9 6 9 5 8 6 11 7 11 3 8 3 4 7* 6 3 4 3 4 3 4 ‘1 6 3 4 3 4 3 4 4 6 4 6
4 4 4 4 3 5 4 4 4 5 5 13 9 13 8 8 8 13 8 8 9 13 13 -2 3
1 1 1 1 1 1 1 1 1 1 1 a6 2 2 2 2-2-2 2 2--
25 26
25 -
2Ssa 30s3 64 66 66 17 2672 -
1153 245a 25= 4.3 61 91
19
19
24 24 24 25 25 26 20
23
24 24
20 20
-
-
-
-
-
-
54 53 53 54 52 54 53 51 54 52 52 55 56 57 58 58 58 57 58 58 56 59 59
82~. para-r-Casein A 83a. para-&asein B 83b. para-r-Casein B 83~. para-r-Casein B 84. Catalase 85. Catalase 86. Catalase 87. Cellulase 88a. Ceruloplasmin I 88b. Ceruloplasmin IIa 88~. Ceruloplasmin IIb 88d. Ceruloplasmin IIIb 88e. Ceruloplasmin 89a. Ceruloplasmin, component I 89b. Ceruloplasmin, component II 90a. Ceruloplasmin I 90b. Ceruloplasmin II 91. Chloroperoxidase 92. Chlorophyll a-Protein 93. Chloroplast coupling factor 94. Chloroplast fraction I protein 95a. Chorismate mutase-prephenate dehydrogenase
67 85
89
48 49 12 19
18
18
50
56 65
64
62 66 24 30
2391
18
80
85 94
100
93 93 14 34
21
20
58
5 9 9 5 141 156 148 24 64 66 70 67
9 14 13 9 154 157 169 38 55 56 55 57
1 3 3 1 155 154 149 46 84 86 85 86
69
19
24
87 87 20 35
89
79 90
780 12 12 780 154 162 137 26 70 78 77 80
35
10
17
28 25 9 20
64
34
12
10
66 69 23 15
79
56 57 a7 77
613 10 19 9 18 613 79 166 85 167 84 176 14 25 53 54 55 55 58 54 60 52
36
11
15
84 87 33 17
91
69 93
7 11 10 7 97 104 105 39 73 68 66 66
36
14
18
74 75 17 16
92
86 92
3 6 6 3 96 107 108 41 88 87 83 87
69
18
19
150 154 39 26
165
135 136
7 11 11 7 294 266 286 53 143 136 137 137
82
21
35
160 170 26 24
134
130 145
18 27 27 18 197 213 231 32 133 131 133 129
-
-
-
8
4
1
2 1
-
17
4
7
26 23 2 4
15@ 26 25
2 2
1 2 2 1 29 41 44 208’ 52 14 4 13 26 15 27 12 26 15 20
-
34
12
11
82 84 4 9
92
68 83
7 9 10 7 116 126 121 19 70 71 70 72
41
10
16
33 33 6 11
44
46 46
5 7 7 5 130 121 126 17 43 44 44 42
16
6
2
39 37 7 15
42
43 43
27
10
7
58 51 13 21
83
54 71
3 4 4 6 5 6 3 4 89 132 70 120 81 128 7 16 44 55 45 55 44 56 46 58
20
9
7
56 54 10 8
76
71 71
9 13 12 9 86 80 80 19 68 71 69 310 -a -s3 -4 -a5
-33 16 -
--
--
8 -
20 20
-
-
71
70
69
67 67 68 16
66
65 66
60 59 59 60 61 61 62 63 64 64 64 64
continued
76
24
160 160 298V 33
162%
160 16Za8
250 250 256 49 160 160 160 160
Table
30z 16
3 -N
-
19 150
27 20 273
24 24
2 2
--
103d.
103~.
103b.
97. 98. 99a. 99b. 100. 101. 102. 103a.
96.
95c.
95b.
Chorismate mutase-prephenate dehydrogenase Chorismate mutase-prephenate dehydrogenase Chromaffin granule protein Chymopapain B Chymosin Chymotrypsin C, Chymotrypsin C Chymotrypsin II Chymotrypsin Chymotrypsin Chymotrypsinogen A Chymotrypsinogen B Chymokypsinogen C Chymotrypsinogen C
30
m
22
41 25 27 25 25 21 22 105
52
60
62
18
15
22
23
23
24
22
109 108
26 16 ‘07 18
16 19 21 19 18g6 21
50
17 21
25
55
72
27 21 23 19 22 20
51
81
73
20 13 93 12 24 97
54
86
14
15 15
14 12 15 12 15 100
68
33
37
5
15
14 111
11
12 10
13 15 14 21 11 11
7
39
38
26
“2
28
19 23
24 27 22 20 21 101
55
34
38
TABLE
17
17
17
18 19
17 18 16 14 19 102
19
37
39
32
2. 5
20
23 20
29 30 259” 22 23 9s
56
73
74
30
2s
26
15
21 16
30 29 25 21 18
156
87
87
2 (Coontinued)
10
10
10
10 10
11 6 10 7 8 g104
3
8
8
57
35
36
1
1
2
3 2
9
7
6
13 11
1 27 7 8 1 7 1 7 2 16 1’0.3 99
13
18
18
9
9
8
10 5 8 7 8473 7 3 5
42
44
41
6
6
3
t5 3 2
5 4 6 5
13
17
17
6
4
8
3 7 106
7 14 4 4
11
25
28
8
6
4
8 3 5
20 15 6 6
8
19
21
14
12-
13-
6 4 12 8 5-7 68
-
16
14
29 31
70
24
-
-
7 -
9 -
32
29
26
26 25 25
24
Q6
35 31
77
82
82
77
82
82
74 75 76 77 78 79 80 81
73
72
72
Chymotrypsinogen Chymotrypsinogen A Chymotryp sinogen A Chymotrypsinogen B Chymotrypsinogen B Chymotrypsinogen B Cocoonase Cocoonase
22 26
16 16
20 19
25
23
23
24
23
23
24
23
23 22
22
22
23 22
22
23
21 22
12 15
19
19
19
19
11 19
12 14
9
8
9
10
10 10
9 10
13
15
13
9
14 9
23 18
22
22
21
25
21 29
4 6 2
119
13 12
11
11
11
4 4
14
10 13
2
4 2
10116 4
10
10
10”s
8 10
7
7
4 5 4120 4
2
5
7
6 9
2
5
G
2
2
4
3 6
5
4 2
7 4
9 9
3
3
3
4
6 4
I4 63 residues of hydroxylysine. 15 No corrections for losses during hydrolysis, I6 Threonine and methionine sulphone. 17 30-31 residues. r8 13-14 residues. I9 11-12 residues. r0 13-14 residues. 21 8-9 residues. 22 16-17 residues. 23 28-29 moles. 24 26 moles (alkaline hydrolysis). 25 Number of residues based on assumption glycine. 28 22 moles by alkaline hydrolysis. 27 One Zn atom/mole. 28 24 moles by alkaline hydrolysis.
15 14
26 23
16 15
19
20117 18”8
20
22
19
15r1”
13 15
23
20
23’13
23 20
20 22
14 22
1 11-12 residues. la - not determined. z 2-3 residues. 3 Fifteen mole y0 N&; one manganese atom; l-2 glucosamine per molecular weight. 4 One mole FAD/50,000 g. 6 Three glucosamine per mole. GEleven glucosamine per mole, 19-12 cysteine residues, 3-4 cystine residues. r One cystine residue. 8 Values for residues normalized to make alanine = 15. No corrections for partial destruction of amino acids. 9 4-5 residues. 10 5-6 residues. r1 2-3 residues. r2 5-6 residues. 13 130 residues of 4-hydroxyproline.
107~ 107b.
106~.
106a. ) bb 106b.
105b.
‘r104. 105a.
16
18
16
21
23 24
26
26
25
26
25 25
Table
89 90
88
87
86
of
85’16
83 84
continued
of 16 residues
3 27 2 -
8
8
6
5
12 20 7-
28 Number of residues based on assumption of 22 residues of alanine. “Number of residues based on assumption of 3 residues of methionine. 81 Number of residues based on assumption of 17 residues of alanine. QNumber of residues based on assumption of 19 residues of alanine. 33 Two residues of amino sugar, 19 of hexose and 3 of fucose. 34 44 residues of hexose, 2 of fucose and no ammo sugar. H Five residues of amino sugar, 15 of hexose and 2 of fucose. 88 Six residues of ammo sugar, 17 of hexose, 2 of fucose. 37 The number of residues based on 81.3% recovery of weighed out sample. 38 The number of residues based on 99% recovery of weighed out sample (Ref 40, footnote d of Table 1) actually correspond to 95% recovery. 89 Two residues of amino sugar, 8 of hexose and 2 of fucose. 40 Results based on glycine to alanine ratio of 22:22 per molecule. 41 Eight residues of serine phosphate. (2 Eight residues of asparagine. W 14 residues of glutamine. u 12 phosphate groups. u 43-49 residues. (6 11-12 residues. 4r 11 phosphate groups. 48 Number of residues based on assumption of 4 residues of
TABLE arginine. 48 Uncorrected for decomposition; 1 disulfide 34,000 molecular weight. 6o 10-11 residues. s1 Uncorrected for decomposition. b* 2-3 residues. b3 Five atoms phosphorus. M 33-34 residues. SKWhole number residues per molecule containing 66 9-10 residues. 67 36-37 residues. 68 32-33 residues. 69 32-35 residues. m 21-22 residues. 61 Four atoms phosphorus. 62 38-39 residues. 63 17-18 residues. M 3-4 atoms phosphorus. 65 One atom phosphorus, 1 mole hexose. 66 l-2 residues. 67 20-21 residues. 68 18-19 residues. 69 3940 residues. r0 12-13 residues. ‘I 4-5 residues. 72 l-2 atoms phosphate. ‘3 12-13 residues. r4 13-14 residues.
2 (Continued)
5 glycine.
group
per
2
3
.Ej: w 3 z x
76 10-11 residues. 7q 11-12 residues. 77 8-Q residues. 78 4-5 residues. 79 True value believed to be 2 residues. 80 Each value adjusted so that value for leucine was 7. 81 Eight residues cysteine, 6 residues cystine. 82 32 moles mannose, 18 moles galactose, 3 moles fucose, 11 moles sialic acid, 16 moles hexoseamine, 28 moles glucoseamine. 83 17 moles mannose, 12 moles galactose, 1 mole fucose, 7 moles sialic acid, 10 moles hexoseamine. 84 20 moles mannose, 11 moles galactose, 2 moles fucose, 6 moles sialic acid, 17 moles hexoseamine, 9 moles glucoseamine. 86 23 moles mannose, 15 moles galactose, 3 moles fucose, 9 moles sialic acid, 17 moles hexoseamine, 9 moles glucoseamine. 86 One residue cysteine and 7 residues cystine. 8’ 57-64 residues. 8* 3% carbohydrate. 89 Without tryptophan, plus hemin. 90 4-5 chlorophyll a per mole; 1 mole carotenoid per 14 moles chlorophyll a. 91 All values normalized to 23 residues alanine. Q2 Based on 3 moles of tryptophan. 83 13-14 residues. Q4 All asparagine residues. 85 28,000-29,000.
w
0
$ F $ F;3
% u
3
116 Five cystine residues. 1x6 Calculated from sequence. 117 Seven asparagine residues. 11s Ten glutamine residues. 110 l-2 residues. 120 Amino acid analysis based residues.
111 13-14
on
assumption
of 4 histidine
E
8 %
of
112 22-23 residues. 113 11 asparagine residues. 114 10 glutamine residues.
mole
E
!?
per
of 18 leucine
residues.
96 Number of residues based on an assumed value residues. 97 16-17 residues. 98 20-21 residues. @g5-6 residues. 100 9-10 residues. 101 32-33 residues. 102 18-19 residues. 103Number of residues based on one methionine enzyme. lo4 Seven residues of cysteic acid formed. 10420-21 residues. 106 5-6 residues. IO7 23-24 residues. 108 16-17 residues. 109 24-25 residues. 110 26-27 residues.
252
DONALD
M.
KIRSCHENBAUM
ACKNOWLEDGMENTS I should like to express my thanks to the Marine Biological Laboratory, Woods Hole, Mass. for the use of their excellent library facilities during July and August, 1971 and July and August, 1972. The Library of the Downstate Medical Center, College of Medicine, has always been the prime source for the data compiled in this series of papers. I should like to thank the staff for their assistance. REFERENCES 1. 2. 3. 4.
FOR
TEXT
KIRSCHENRAUM, D. M. (1971) Anal. Biochem. 44, 159. KII(SCHENBAUM, D. M. (1972) Anal. Biochem. 49, 248. SPENCER, R. L., AND WOLD, F. (1969) Anal. Biochem. 32, 185. TANIS, R. J., TASHIAN, R. E, AND Yu, Y. S. L. (1970) J. Biol. REFERENCES
FOR
TABLE
Chem.
245,
6003.
2
1. CABAN, C. E., AND HASS, L. F. (1971) J. BioZ. Chem. 246, 6807. 2. DIKOW, A. L., JECICEL, D., AND PFLEIDERER, G. (1971) Hoppe-Seyler’s 2. Physiol. Chem. 352, 1151. 3. ‘S-GRAVENMADE, E. J., VAN DER DRIFT, C., AND VOGELS, G. D. (1971) Biochim. Biophys. Acta 251, 393. 4. KOTAKI, A., HARADA, M., AND YAGI, K. (1967) J. Biochem. (Tokyo) 61, 598. 5. Dons, D. (1971) J. BioZ. Chem. 246, 4965. 6. SANDERS, T. G., AND RUTTER, W. J. (1972) Biochemistry 11, 130. 7. HENDERSON, E. J., AND ZALKIN, H. (1971) J. BioZ. Chem. 246, 6891. 8. SPRINGER, G. F., AND DESAI, P. R. (1971) Biochemistry IO, 3749. 9. BRYCE, C. F. A., AND CRICHTON, R. R. (1971) J. BioZ. Chem. 246, 4198. 10. SANDERMANN, JR., H., AND STROMINGER, J. L. (1971) Proc. Nat. Acad. Sci., U. S. A. 68, 2441. 11. HIRSCH-K• LB, H., AND GREENBERG, D. M. (1963) J. BioZ. Chem. 243, 6123. 12. BRAY, R. C., AND RATNER, S. (1971) Arch. Biochem. Biophus. 146, 531. 13. BRESMW, J. L., AND SLOAN, H. R. (1972) Biochem. Biophys. Res. Comm. 46, 919. 14. STARK, G. R., AND DAWSON, C. R. (1962) J. Biol. Chem. 237, 712. 15. ICHISHIMA, E., AND YOSHIDA, F. (1965) Biochim. Biophvs. Acta 110, 155. 16. THORNBER, J. P., AND OLSON, J. M. (1968) Biochemistry 7, 2242. 17. DE GRAAF, F. K., GOEDVOLK-DE GROW, 1,. E., APED STIXJTHAMER, A. H. (1970) Biochim. Biophys. Acta 221, 566. 18. CARUSI, E. A., AND SINSHEIMER, R. (1963) J. &lol. Biol. 7, 388. 19. POLJAK, R. J. (1968) Virology 35, 185. 20. POLJAK, R. J., AND SURUDA, A. J. (1969) Virology 39, 145. 21. BUCHWALD, M., STEED-GLAISTER, P., AND SIMINOVITCH, L. (1970) ViroZogy 42, 375. 22. LIN, J. Y., WV, C. C., AND KUE, T. T. (1971) Virology 45, 38. 23. YONEMASU, K., STROUD, R. M., NIEDERMEIER, W., AND BUTLER, W. T. (1971) Biochem. Biophys. Res. Comm. 43, 1388. 24. BTIDZKO, D. B., BOKISCH, V. A., AND MULLER-EBERHARD, H. J. (1971) Biochemistry 10, 1166. 25. MUNN, E. A., FEXNSTEIN, A., AND GREVILLE, G. D. (1971) Biochem. J. 124, 367.
AMINO
ACID
ANALYSES
OF
PROTEINS.
III
253
26. MACLENNAN, D. H., AND WONG, P. T. S. (1971) Proc. Nat. Acad. Sci., U. 8. A. 68, 1231. 27. MARSHALL, M., AND COHEN, P. P. (1966) J. Biol. Chem. 241, 4197. 28. FOLEY, R., POON, J., AND ANDERSON, P. M. (1971) Biochemistry 10, 4562. 29. LAURENT, G., CASTAY, M., MARRIQ, C., GARCON, D., CHARREL, M., ANP DERRIEN, Y. (1963) Biochim. Biophys. Acta 77, 518. 30. LAURENT, G., CHARREL, M., M~RIQ, C., GARCON, D., AND DERRIEN, Y. (1966) Bull. Xoc. Chim. Biol. 48, 1125. 31. NYMAN, P. O., AND LINDSKOG, S. (1964) Biochim. Biophys. Acta 85, 141. 32. RICKLI, E. E., GHAZANFAR, S. A. S., GIBBOKS, B. H., AND EDSALL, J. T. (1964) J. Bid Chem. 239, 1065. 33. ARMSTRONG, J. M., MYERS, D. V., VERPOORTE, J. A., AND EDSALL, J. T. (1966) J. Biol. Chem. 241, 5137. 34. CARTER, M. J. (1971) Biochim. Biophys. Acta 235, 222. 35. ASHWORTH, R. B., BREWER, J. M., AND STANFORD, JR., R. L. (1971) Biochem. Biophys. Res. Comm. 44, 667. 36. TANIS, R. J., AND TASHIAN, R. E. (1971) Biochemistry 10, 4852. 37. CARTER, M. J., AND PARSONS, D. S. (1970) Biochem. J. 120, 797. 38. DUFF, T. A., AND COLEMAN, J. E. (1966) Biochemistry 5, 2009. 39. MAYNARD, J. R., AND COLEMAN, J. E. (1971) J. Biol. Chem. 246, 4455. 40. KLAPP, B., KRISCH, K., AND BORNER, K. (1970) Hoppe-Seyler’s 2. Physid. Chem. 351, 81. 41. REECK, G. R., WALSH, K. A., AND NEURATII, H. (1971) Bioch.emistry 10, 4690. 42. PLUMMER, JR., T. H. (1971) J. Biol. Chem. 246, 2930. 43. PRAHL, J. W., AND NEURATH, H. (1966) Biochemistry 5, 4137. 44. GORDON, W. G., BASCH, J. J., AND THOMPSON, M. P. (1965) J. Dairy Sci. 48, 1010. 45. MERCIER, J. C., GROSCI.AUDE, F., AND RIBADEAU-DUMAS, B. (1971) Europ. J. Biochem. 23, 41. 46. DE KONING, P. J., AND VAN ROOIJEN, P. J. (1965) Biochem. Biophys. Res. Comm. 20, 241. 47. DE KONING, P. J., AND VAN ROOIJEN, P. J. (1967) Nature 213, 1028. 48. THOMPSON, M. P. (1971) in Milk Proteins, Chemistry and Molecular Biology. II (H. A. McKenzie, ed.), p. 117. Academic Press. New York. 49. HOAGLAND, P. D., THOMPSON, M. P., AND KALAN, E. B. (1971) J. Dairy Sci. 54, 1103. 50. MANSON, W., AND ANNAN, W. D. (1971) Arch. Biochem. Biophys. 145, 16. 51. PION, R., GARNIER, J., RIBADEAU-DUMAS, B., DE KONING, P. J., AND VAN ROOIJEN, P. J. (1965) Biochem. Biophys. Res. Comm. 20, 246. 52. GROVES, M. L., AND GORDON, W. G. (1969) Biochem. Biophys. Acta 194, 421. 53. PETERSON, R. F., NAUMAN, I,. pi’., AND HAMILTON, D. F. (1966). J. Dairy Sci. 49, 601. 54. THOMPSON, M. P., GORDON, W G., PEPPER, L., AND GREENBERG, R. (1969) Camp. Biochem. Physiol. 30, 91. 55. JOLLES, P., ALAIS, C., AND JOLLES, J. (1962) Arch. Biochem. Biophys. 98, 56. 56. KALAN, E. B., AND WOYCHIK, J. H. (1965) J. Daily Sci. 48, 1423. 57. SCHMIDT, D. G., BOTH, P., AND DE KONING, P. J. (1966) J. Dairy Sci. 49, 776. 58. WOYCHIK, J. H., KALAN, E. B., AND NOELKEN, M. E. (1966) Biochem&Ty 5, 2276. 59. DE KONING, P. J., VAN ROOIJEN, P. J., AND KOK, A. (1966) Biochem. Biophys. Res. Comm. 24, 616.
254
DONALD
M.
KIRSCHENBAUM
60. KIM, Y. K., YAGUCHI, M., AND ROSE, D. (1969) J. Dairy Sci. 52, 316. 61. SCHROEDER, W. A., SAHA, A., FENNINGER, W. D., AND CUA, J. T. (1962) Biochim. Biophys. Acta 58, 611. . 62. HIQASHI, T., AND SHIBATA, Y. (1964) J. Biochem. (Tokyo) 56, 361. 63. DATTA, P. K., HANSON, K. R., AND WHITAKER, D. R. (1963) Can. J. Biochem. Physiol. 41, 697. 64. RYDEN, L. (1971) Znt. J. Protein Res. 3, 131. 65. KASPER, C. B., AND DEUTSCH, H. F. (1963) J. Biol. Chem. 238, 2325. 66. KAYA, T. (1964) J. Biochem. (Tokyo) 56, 122. 67. VASILETS, I. M., SHAVLOVSKII, M. M., AND MUKKA, G. V. (1970) Biochemistry (U.SS.R.) 35, 986. 68. MORRIS, D. R., AND HAGER, L. P. (1966) J. Biol. Chem. 241, 1763. 69. FARRON, F. (1970) Biochemistry 9, 3823. 70. RIPLEY, S. M., THORNBER, J. P., AND BAILEY, J. L. (1967) B&him. Biophys. Acta 140, 62. 71. KOCH, G. L. E., SHAW, D. C., AND GIBSON, F. (1970) Biochem. Biophys. Acta 212, 375. 72. KOCH, G. L. E., SHAW, D. C., AND GIBSON, F. (1971) Biochim. Biophys. Acta 229, 795. 73. SMITH, A. D., AND WINDLER, H. (1967) Biochem. J. 103, 483. 74. KUNIMITSU, D. K., AND YASUNOBU, K. T. (1970) Methods Enzymol. 19, 244. 75. FOLTZMANN, B. (1964) Compt. R. Trav. Lab. Curlsberg 34, 275. 76. GRATECOS, D., AND DESNUELLE, P. (1971) Biochem. Biophys. Res. Comm. 42, 857. 77. FOLK, J. E., AND SCHIRMER, E. W. (1965) J. Biol. Chem. 240, 181. 78. COAN, M. H., ROBERTS, R. C., AND TRAVIS, J. (1971) Biochemistry 10, 2711. 79. RYAN, C. A., CLARY, J. J., AND TOMINATSU, Y. (1965) Arch. Biochem. Biophys. 110, 175. 80. VANDERMEERS, A., AND CHRISTOPHE, J. (1969) Biochim. Biophys. Acta 188, 101. 81. CHARLES, M., GRATECOS, D., ROVERY, M., AND DESNULLE, P. (1967) Biochem. Biophys. Acta 140, 395. 82. GRATECOS, D., GUY, O., ROVERY, M., AND DESNIJELLE, P. (1969) Biochim. Biophys. Acta 175, 82. 83. PRAHL, J. W., AND NEURATH, H. (1966) Biochemistry 5, 2131. 84. ZMRHAL, Z. (1962) Collect. Czech. Chem. Commun. 27, 2662. 85. HARTLEY, B. S. (1970) Phil. Trans. Roy. Sot. London Ser. B 257, 77. 86. SMILLIE, L. B., ENENKEL, A. G., AND KAY, C. M. (1966) J. BioZ. Chem. 241, 2097. 87. GUY, O., GRATECOS, D., ROVERY, M., AND DESNULLE, P. (1966) Biochem. Biophys. Acta 115, 402. 88. SMILLIE, L. B., FIJRKA, A., NAGABHUSHAN, N., S~VENSON, K. J., AND PARKES, C. 0. (1968) Nature 218, 343. 89. KAFATOS, F. C., TARTAKOFF, A. M., AND LAW, J. H. (1967) J. BioZ. Chem. 242, 1477. 90. HRUSKA, J. F., AND LAW, J. H. (1971) Methods Enzymol. 19, 221.
BIOCHEMISTRY
A Compilation
52, 234-264
of Amino DONALD
Department
of Biochemistry,
Received
(1973)
Acid
Analyses
of Proteins.
III
M. KIRSCHENBAUM
College of Medicine, Downstate Brooklyn, New York 11205
September
8, 1972;
accepted
October
Medical
Center,
10, 1972
In this paper, the third of the series (1,2), I have added an additional 173 proteins for which amino acid analyses have been published. The molecular weights have been rounded off to the nearest hundred for weights under 10,000 and to the nearest thousand for weights above 10,000. The number of residues have been rounded off to the nearest integral number. Methods of analysis are those described previously (1,2), and occasionally cysteine was determined using the dimethyl sulfoxide procedure (3) or by reaction with 2-bromoacetamido-4-nitrophenol (4). Table 1 is the Protein Index and gives the names of the proteins, the enzyme commission numbers supplied by the references cited, and the sources of the proteins. Table 2 gives the amino acid analysis, amide ammonia, molecular weight, and literature citat,ion. Aspartic acid includes asparagine residues converted to aspartic acid during hydrolysis. Glutamic acid includes glutamine residues converted to glutamic acid during hydrolysis. TABLE Number 1.
2a. 2b. 2c. 3.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
Aldolsse, fructose 1,6diphosphate Mustelus canis (shark) Aldolase A, EC 4.1.2.7 Human muscle Aldolase B, EC 4.1.2.7 Human liver Aldolase C, EC 4.1.2.7 Human brain Allantoicase, 30% 0.9s + 70% 10.85 Pseudomonas aeruginosa (a bacterium)
Copyright
@ 1973 by
All
of
riehts
1: Protein
rmvm+~rtinn
Academic in
Press, REV
fnrm
Index 4.
Name:
5.
Source: Name:
6a.
Source: Name:
6b.
Source: Name: Source:
7.
234 Inc. r~=~=rv~d
Name:
n-Amino acid oxidase, EC 1.4.3.3 Pig kidney &Aminolevulinate dehydratase, EC 4.2.1.24 Mouse liver or-Amylase (IEP = 8.95), EC 3.2.1.1 Rat pancreas cY-Amylase (IEP = 8.77), EC 3.2.1.1 Rat pancreas Anthranilate wynthetase: anthranilate 5-PRPP
AMINO
ACID
ANALYSES
TABLE
Source:
8. Name: Source: 9. Name: Source: 10. Name: Source: 11. Name: Source: 12a. Name: 12b.
Source: Name:
13.
Source: Name:
Source: 14. Name: Source: 15a. Name: Source: 15b.
16.
Name: Source: Name:
Source:
phosphoribosyltransferase Salmonella typhimurium (a bacterium) Antibody, anti-human blood group H(0) Anguilla rostrata (eel) Apoferritin Horse spleen Apoprotein, C&-isoprenoid alcohol phosphokinase Staphylococcus aureus membrane Arginase, EC 3.5.3.1 Rat liver Argininosuccinase, EC 4.3.2.1 Bovine kidney Argininosuccinase, EC 4.3.2.1 Bovine liver Arylsulfatase A, monomer Human urine Ascorbic acid oxidase Corcubita pepo condensa (yellow crookneck squash) Aspergillopeptidase A Aspergillus
satoi
(a common mold) Aspergillopeptidase Aspergillus
A
satoi
OF
PROTEINS.
1 (Continued) 19b.
Name:
19~.
Xame:
20a.
Source: Name:
Source:
Source: 20b.
Name: Source:
21a. Name: Source:
Zlb.
Name: Source: 21~. Name: Source: 22. Name: Source: 23.
Name: Source:
24a.
Name: Source: 24b. LVame: Source: 24~. Name: Source: 24d. Name: Source: 25. Name: Source..
(a common mold) Bacteriophyll-protein complex
26.
Name: Source:
Chloropseucbmonas ethylicum (a bacterium)
27.
Name:
17. Nqe: Bacteriocm DF13 Source: Enterobacter cloacae (a bacterium) 18. Name: Bacteriophage +x174, protein Source: Bacteriophage 4x174 19a. Name: Bacteriophage 6x174 particle Source: Bacteriophage 6x174
235
III
28.
29.
Bacteriophage subunit o Bacteriophage Bacteriophage subunit p Bacteriophage Bacteriophage particle Bacteriophage Bacteriophage subunit B Bacteriophage Bacteriophage Bacteriophage Bacteriophage Bacteriophage Bacteriophage Bacteriophage Bacteriophage protein Bact.eriophage Ch Human serum
+x174, +x174 9x174, +x174 S13 S13 S13, S13 h ghosts h X heads X x tails x xf coat xf
c3
Human serum C3a (C4,2) Human serum C3a(Try) Human serum C3a(NH20H) Human serum Calliphorin Calliphora erythrocephala (blowfly) Calsequestrin Rabbit sarcoplasmic reticulum Carbamate kinase, EC 2.7.2.2
Source:
Streptococcus
Name:
(a bacterium) Carbamyl phosphate synthetase
faecalis
Source:
Escherichia
Name: Source:
(a bacterium) Carbonic anhydrase X, Human erythrocyt,es
coli
236
DONALD
M.
TABLE 30. 31. 32. 33. 34.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
35a. 35b. 36.
Name: Source: Name: Source: Name: Source:
37. 38. 39. 4th
Name: Source: Name: Source: Name: Source: Name: Source:
40b.
Name:
44a.
Source: Name: Source: Name: Source: Name: Source: Name:
44b.
Source: Name:
45a.
Source: Name:
45b.
Source: Name:
45~.
Source: Name:
41. 42. 43.
Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Human erythrocytes Carbonic anhydrase Bovine erythrocytes Carbonic anhydrsse low activity Bovine rumen Carbonic anhydrase low activity Bovine rumen Carbonic anhydrase Deer erythrocytes Carbonic anhydrase Goat erythrocytes Carbonic anhydrase Sheep erythrocytes Carbonic anhydrase, major component Sheep erythrocytes Carbonic anhydrase, minor component Sheep erythrocytes Carbonic anhydrase, low activity Guinea pig erythrocytes Carbonic anhydrase, high activity Guinea pig erythrocytes Carbonic anhydrase,
KIRSCHENBAUM 1 (Continued)
Y A 46a.
Source: Name:
B Source: B 46b.
Name:
B Source: B 47. B 48a. C 48b. C 49. C B
50.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
a, 51a.
Name:
51b.
Source: Name:
51~.
Source: Name:
51d.
Source: Name:
52.
Source: Name:
b,
C C
C
SOUTCe:
53a. 53b.
Name: Source: Name:
53~.
Source: Name:
54a.
Source: Name: Source:
secondary high activity isozyme Guinea pig erythrocytes Carbonic anhydrase, low activity Guinea pig colonic mucosa Carbonic anhydrase, high activity Guinea pig colonic mucosa Carbonic anhydrase Guinea pig stomach Carbonic anhydrase B Macacu mu&a (monkey) Carbonic anhydrase C Macuca mulata (monkey) Carbonic anhydrase Galwcerclo cuvieri (tiger shark) Carbonic anhydrase Carcharhinus leucas (bull shark) Carboxylesterase, EC 3.1.1.1 Pig liver Carboxylestersse EC 3.1.1.1 Pig liver Carboxylesterase EC 3.1.1.1 Pig kidney Carboxylesterase EC 3.1.1.1 Pig kidney Carboxylesterase EC 3.1.1.1 Bovine liver Carboxypeptidase BI Bovine pancreatic juice Carboxypeptidase BI, heavy chain Bovine pancreatic juice Carboxypeptidase BI, light chain Bovine pancreatic juice Carboxypeptidase BII Bovine pancreatic juice
AMINO
ACID
ANALYSES
TABLE 54b.
Name:
54c.
Source: Name:
55. 56. 57. 58a. 58b. 58~. 59a. 59b. 60. 61. 62a. 62b. 63a. 63b. 64. 65. 66. 67a. 67b.
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: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name:
Source: 68a. Name: Source:
Carboxypeptidase heavy chain Bovine pancreatic Carboxypeptidase light chain Bovine pancreatic Carboxypeptidase Bovine Carboxypeptidase Squalus acunthias Pacific dogfish) cd2asein A Bovine milk oc.$&sein B Bovine milk orJ1-Casein B Bovine milk or,&asein B Bovine milk cy,&!asein C Bovine milk c.&&sein C Bovine milk ol,l-Casein BC Bovine milk ~&asein D Bovine milk a,,&asein Bovine milk aB,&asein Bovine milk a..&asein Bovine milk or,,r-Casein Bovine milk cr,,.&asein Bovine milk @-Casein Bovine milk @-Casein A Bovine milk j%Casein A1 Bovine milk @Casein A1 (HissAspoGlua) Bovine milk &Ca.sein A* Bovine milk
OF
PROTEINS.
III
1 (Continued)
BII,
68b.
Name:
juice BII,
68~.
Name:
juice B
68d.
Name:
B (spiny
69a.
Source:
Source:
Source:
69c.
70a. 70b. 7oc. 71a. 71b. 71c. 71d.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
72. Name: Source: 73. Name: Source: 74. Name: Source: 75. Name: Source: 76. Name: Source: 77. Name: Source: 78a. Name: Source: 78b. Name: Source:
@-Casein AZ-1 (His&p,~Glu& Bovine milk p-Casein Azde (Hisdsp~~Glud Bovine milk @%.sein AZ+ (H~wQJPQG~u~~) Bovine milk @-Casein B Bovine milk &Cssein B Bovine milk &Casein B Bovine milk p-Casein B-l Bovine milk fMa.sein B-2 Bovine milk B-Casein B. Bovine milk p-Casein C Bovine milk p-Casein C Bovine milk @Casein C Bovine milk fi-Casein C Bovine milk (Abondance cow Simmental type) p-Casein D Bovine milk r-Casein A2 Bovine milk &asein B Bovine milk K-Casein Bovine milk K-Casein Bovine milk K-Casein A Bovine milk K-Casein A-l Bovine milk &&sein A-2 Bovine milk
237
238
DONALD
M.
TABLE 78~. 79. 80a. 80b. 81. 82a. 82b. 82~. 83a. 83b. 83~. 84. 85. 86. 87. 88a.
88b. 88~. 88d. 88e. 89a.
89b.
&asein A-4 Name: source: Bovine milk Name: K-Casein B Bovine milk Source: Name: K-Casein B-l Bovine milk Source: Name: dhsein B-2 Bovine milk Source: Name: para-&asein Source: Bovine milk para-K-c&S& A (0.60) Name: Source: Bovine milk para-r-Casein A Name: Source : Bovine milk Name: paTa-K-CaSein A Bovine milk Source: Name: para-r-Casein B (0.52) Source: Bovine milk Name: para-r-Casein B Bovine milk Source: Name: pa?U-K-&S& B Source: Bovine milk Catalase Name: Source: Bovine liver Name: Catalase Source: Horse liver Name: Catalase Source: Rat liver Name: Cellulase Source: Myrothecium verrucaria Ceruloplasmin I Name: (Cohn IVa) Human plasma Source: Name: Ceruloplasmin IIa Source: Human plasma Ceruloplasmin IIb Name: Human plasma Source: Name: Ceruloplasmin IIIb Source: Human plasma Name: Ceruloplasmin Source: Human plasma Ceruloplasmin, Name: component I Source: Pig serum Name: Ceruloplasmin, component II Source: Pig serum
KIRSCHENBAUM 1 (Continued) 9Oa. 90b. 91. 92.
Name: Source: Name: Source: Name: Source: Name: Source:
93.
Name:
94.
Source: Name: Source:
95a.
Name:
Source: 95b.
Name:
Source: 95c.
Name:
Source: 96.
97. 98. 99a. 99b. 100. 101. 102.
Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source: Name: Source:
Ceruloplasmin I Albino rat Ceruloplasmin II Albino rat Chloroperoxidase Calduriomyces fumago Chlorophyll a-Protein Beta vulgaris (spinach beet) chloroplasts Chloroplast coupling factor; CF, Spinach chloroplasts Chloroplast fraction I protein Beta vulgaris (spinach beets) chloroplasts Chorismate mutaseprephenate dehydrogenase Aerobacter aerogenes (a bacterium) Chorismate mutaseprephenate dehydrogenase Aerobacter agogenes (a bacterium) Chorismate mutaseprephenate dehydrogenase Escherichia wli (a bacterium) Chromaffin granule protein Bovine adrenal medulla Chymopapain B Papaya Chymosin Calf stomach Chymotrypsin C. Pig pancreas Chymotrypsin C Pig pancreas Chymotrypsin II Human pancreas Chymotrypsin Chicken pancreas Chymotrypainogen Rat pancreas
AMINO
ACID
ANALYSES
TABLE 103~~. Name: Source: 103b. Name: Source: 103~. Name: Source: 103d. Name: Source: 104. Name: Source: 105a.
Name: Source:
Chymotrypsinogen A Pig pancreas Chymotrypsinogen B Pig pancreas Chymotrypsinogen C Pig pancreas Chymotrypsinogen C Pig pancreas Chymotrypsinogen Squalus acunthias (spiny Pacific dogfish) Chymotrypsinogen A Bovine pancreas
OF
PROTEINS.
III
239
1 (Continued) 105b.
Name: Source: 106a. Name: Source: 106b. Name: source:
106~. Name: Source: 107a. Name: Source: 107b.
Name: Source:
Chymotrypsinogen A Bovine pancreas Chymotrypsinogen B Bovine pancreas Chymotrypsinogen B Bovine pancreas Chymotrypsinogen B Bovine pancreas Cocoonase Anthe-raea pernyi (Chinese oak silk moth) Cocoonase Antheraea polyphemus
8. 9. 10. 11. 12a. 12b. 13. 14.
6a. 6b. 7.
5.
1. 2a. 2b. 2~. 3. 4.
acid
Aldolase Aldolase A Aldolase B Aldolase C Allantoicase ~-Amino acid oxidase &Aminolevulinate dehydratase a-Amylase a-Amy&e Anthranilate synthetase Antibody Apoferritin Apoprotein Arginase Argininosuccinsse Argininosuccinsse Arylsulfatase A Ascorbic acid oxidase
Amino
92 10 9 90 124 121 124 94
51 52 170
22
124 130 117 129 10 43
A Compilation
89 14 14 64 156 151 62 76
35 35 274
29
1 35
173 186 180 181
29
108 156 147 135 8 47
66 55 725 11 23 86 71 102 209 98 202 50 50 79 91
35 24 36 23 135 254
6
78 74 79 91 8 34
of Amino
Acid
12
58 42 3 3 23 4 51 71 60 62 59 61 25 149 72 92
24 21 23 20 85 106
7
90 74 83 113 77 90 73 104 4 5 19 16
Analyses
74 9 8 60 141 139 74 73
33 35 131
14
67 86 79 75 5 17
74 5 8 68 96 96 37 70
24 24 123
14
116 83 65 72 5 29
110 17 8 87 143 138 74 132
86 81 232
17
107 102 111 117 10 34
TABLE of Proteins
90 24 8 87 199 191 112 100
32 34 251
31
154 170 177 165 10 45
46 3 0 7 17 16 18
10 10 53
28
32 -a 1 16
2 (in residues
6 3 4 13 53 51 12 17
10 11 61
7
6
27 16 27 15 a
31 9 8 87 73 76 50 55
27 26 72
12
109 142 128 109 5 19
per molecular
13 13 65
6
43 38 40 28 2 12
53 38 9675 53104 33 23 110 45 116 47 37 39 37 39
28 26 137
14
51 69 65 83 4 28
weight
29
24 36 36 12 50
31 52 51 25 53
16 16 57
8
47 54 41 47 2 15
18
26 25 68
12
44 35 42 39 4 17
of protein)
8 181
6 -
12 110 310 35
10 130 2-19 412 35 35 50 -
-
-
17 118 190 188 110 -6
1236
56 56 280
40
160 160 160 160 113 504
8 9 10 11 12 12 13 14
67
6
5
4
22 2 3
1
ii
F w i;i :: X g t?
5
8
23. 24a. 24b. 24~.
22.
21~.
21b.
21a.
2Ob.
20a.
19c.
19b.
19a.
16. 17. 18.
15b.
15a.
Aspergillopeptidase A Aspergillopeptidase A Bacteriophyll Bacteriocin DF13 Bacteriophage 4x174 protein Bacteriophase 6x174 particle Bacteriophage 4x174 subunit Bacteriophage 4x174 subunit Bacteriophage S13 particle Bacteriophage 513 subunit Bacteriophage ?a ghosts Bacteriophage A heads Bacteriophage X tails Bacteriophage xf coat protein Clq C3 C3a(C+ 2) C3a(Try)
580 93 3 3
9
33
20
15
16
18
15
14
16
34 71 17
31
32
148 87 3 3
6
38
25
18
15
15
15
15
16
21
11
16
17
16
17
16
18 29 18
19
20
185 201 129 132 25 34
81
38
25
14
12
13
12
21
14
29 30 14
18 50 15
15
22
22
20
20
19
16
8
16
14
13
16
13
15 39 15
10
10
2
29
20
13
14
15
12
18
14
23 35 15
42
43
I2
40
19
15
14
16
16
17
16
13 25 17
25
25
34
33
18
29
26
23
25
23
33 56 27
34
35
128 20213 18515 17715 285 64 73 94 92 143 13 3 3 4 23 3 3 5
31
10
11
6
9
10
10
8
10
20 16 10
11
12
308 204 6 6
I
30
40
20
17
17
19
14
17
28 54 18
22
22
7
10
5
19
6
6
10
3 7 5
0
0
82 85 34 26 42 42
02
1
1
1
l-
11
1
9
2
2 0 2’
1
1
2
12
18
9
11697--
12
001
1
1
1
6
6
4
512
10
12
6
12
10
13
15 12 11
13
13
7
12
6
9
6
2
Y--
8 12 10
17
18
12314 144 47 142 1O1’6 100 63 25 54 51 5 s121-5 7121--
2
18
17
10
11
10
11
7
9 9
11
7 10 5
3
1 18 23 12
3
1
9
16 51 9
11
11
-
-
-
l-
4 -
2 -
I -
30 -
-
-
-
31
32
4.9
36
34
19
8
*
s
*
*
33 56 26
35
36
23 24 24 24
22
21
21
21
20
20
19
19
19
16 17 18
15
15
continued
388 185 7.2 7.2 Table
5 7 8 6 -
I
1
36.
35b.
35a.
34.
33.
32.
31.
30.
29.
24d. 25. 26. 27. 28.
acid
C3a(NH20H) Calliphorin Calsequestrin Carbamate kinase Carbamyl phosphate synthetase Carbonic anhydrase X, Carbonic anhydrase Y Carbonic anhydrase A Carbonic anhydrase B Carbonic anhydrase B Carbonic anhydrase B Carbonic anhydrase B Carbonic anhydrase B Carbonic anhydrase C
Ammo
22
162”
16
15
16
16
17
24
15
6 193 15 28 148
13
19
19
18
19
20
20
14
19
3 117 26 35 195
17
17
18
17
17
17
17
16
27
20
21
19
20
20
20
29
us 20
36 213 209 27 35 27 27 134 143
9
9
10
10
10
10
10
9
8
18
17
18
15
18
18
18
16
17
22 143 110 20 20 22 16 109 76
19
30
30
27
30
30
30
19
29
4 154 14 14 80
TABLE
13
14
14
13
14
15
15
12
m
29
31
31
31
31
32
31
r’
30
3 5 172r6 426 11 74 16 31 107 182
24
22
22
22
24
25
24
26
22
7-361 72 43 225
2 (Continued)
1
1
1
1
1
1
1
1
1
I
2
2
2
2
2
2
1
2
18 162 3 6 3 6 21 45
25
18
18
18
18
19
19
27
17
5 295 26 24 96
7
7
7
7
7
7
7
8
8
12
11
11
11
11
11
11
lo
11
13
11
11
10
11
11
11
13
IO
9
8
8
8
8
8
8
9
21
9221-116 118 400 442 7 6 24 6 3 6 6 5 LO2 36 71 54
7
6
6
6
6
6
7
7
6
21
26
27
25
272’
27
27
23
za
64 2 34 15 -
3027
29”
3027
2827
30
30
30
32
29
7.8 530 44 31 200
33
33
33
32
31
30
30
29
29
24 25 26 27 28
37. Carbonic anhydrase 38. Carbonic anhydrase 39. Carbonic anhydrase 40a. Carbonic anhydrase 40b. Carbonic anhydrase 41. Carbonic anhydrase 42. Carbonic anhydrase 43. Carbonic anhydrase 44a. Carbonic anhydraae 44b. Carbonic anhydraee 45a. Carbonic anhydrase 45b. Carbonic anhydrase 45~. Carbonic anhydrase 46a. Carbonic anhydrase 46b. Carbonic anhydrase
C
C
C
b
a
B
C
C
20
20
1731
1932
19
17
19
18
18
20
19
19
20
19
24
20
2299
22y9
17
13
13
18
18
21
21
18
18
20
22
22
17
18
18
18
18
22
22
23
23
22
15
16
20
17
17
25
20
24
25
20
26
26
28
28
26
25
25
26
26
25
8
11
8
8
11
3
3
3
5
2
10
10
5
9
9
17
16
17
17
16
23
20
21
21
21
20
20
20
17
17
21
33
24
22
33
15
18
18
18
17
26
26
16
17
19
11
11
12
12
11
9
11
13
12
13
10
10
15
12
13
25
25
25
25
25
32
33
32
32
32
30
30
32
29
29
25
24
25
25
23
24
25
27
26
23
21
22
24
25
27
-
-
-
-
-
1
1
0
0
0
0
1
0
1
1
3
0
3
3
1
330
3='
3
33"
2
1
1
3
1
1
23
19
23
23
19
18
18
19
20
20
20
21
19
24
24
11
11
12
12
13
11
10
11
12
12
5
5
14
5
14
10
6
14
51098
9
10
10
10
11
7
8
9
7
7
11
9
11
11
12
12
12
13
13
11
11
11
12
12
7
8
7
7
6
7
7
7
7
7
7
8
8
8
-
-
-
-
-
-
-
-
-
7 -
6-
-
6 -
6 -
5 -
5 -
7-
7
7
7
Table
2628
21
2196
-
37
37
37
37
37
36
36
35
35
35
34
34
31
30
31
wntinued
28
30
29
28
30
30
-
-
-
30
30
3P'
30
3op1
acid
47. Carbonic anhydrase 48a. Carbonic anhydrase B 48b. Carbonic anhydrase C 49. Carbonic anhydrase 50. Carbonic anhydrase 51a. Carboxylesterase 51b. Carboxylesterase 51~. Carboxylesterase 51d. Carboxylesterase 52. Carboxylesterase 53a. Carboxypeptidase BI 53b. Carboxypeptidase BI 53~. Carboxypeptidase BI 54a. Carboxypeptidsse BII
Amide
19
16
12
23
19
110 109 92 107 115 24
17
7
23
19
15
22
32
30
116 123 107 126 101 23
17
7
22
15
5
10
117 120 95 111 109 16
10
13
14
16
17
21
5
16
143 142 119 139 152 21
32
32
24
19
25
8
15
12
647879214
9
28
21
85 99 28
29
53 98 58 103 15 13
24
12
31
78 SO 73
21
16
30 18
24
49 107 45102 46 84
17 16
18
10 10
8
TABLE
28
20
72 67 28
74 71 61
11
13
13 11
12
28
23
126 129 30
128 120 108
33
40
36 30
25
27
17
144 127 26
155 151 124
41
40
22 26
25
2 (Continued)
-
8
5
10 11 8
17 14 9
25
18
1 1
6
4
31 26 5
25 30 26
2
3
1 2
3
17
14
91 89 17
92 89 78
26
29
18 24
23
12
6
2
4
8
35 32 29
9
14
34 40 5
3
12
13
5
7
69 71 13
71 71 59
12
18
910 12 11
15
49 47 11
45 42 42
10
13
7 8
5
20
2
16
37 34 20
35 37 31
8
9
9 7
7
3627
4027
2827 292’
30
10
4-
6 -
35
10
25
1673* 167= 35
30 18P 167 30 110S4 167 26 1583516737
5 -
7 -
77 -
-
30 185= 53 155 10 -
-
41
41
41
40 40 41
40 40 40
39
39
38 38
37
2
: w Ed 0” Di g $
i
g
E
57. %a. 58b. 5th. 59a. 59b. 60. 61. G2a. 62b. 63a. 63b. 64. 65. 66. 67a. 67b. 68a. 68b. 68~. 68d. 69a. 69b.
56.
55.
54~.
54b.
Carboxypeptidase BII heavy chain Carboxypeptidase BII light chain Carboxypeptidase B Carboxypeptidase B a,,-Casein B a,l-Casein B ol,l-Casein B ol,l-Casein B a,,-Casein C or,&asein C ol,&asein BC c&Za.sein D Ly.,3-Casein ol,,&nsein ay,,&-Caseio ru+-Casein cu,,s-Casein /%Casein &Casein A p-Casein A1 o-Casein A1 @-Casein A? &Casein AZ-l &Casein A2e2 @-Casein AZ+ @-Casein B fi-Casein B
16
10
24
22
11 10 11 11 9 9 11 11 12 I1 12 11 46 11 11 10 2 6 4 11 2 6 4 11 9 24 5 5 5 5 565 5 5 5 556 5 5 6 5 5 5 5 5 5 5 555
20
22
17
22
17
12 17 13 20 11 17 14 21 14 21 14 21 14 21 13 20 10 9 19 17 10 9 20 18 37 37 1921 20 22 18 21 19 21 18 21 19 21 18 21 18 21 20 22 18 21
17
14
7754546879214
16
14 13 11 14 13 14 14 13 8 15 7 15 29 10 10 10 9 10 10 10 9 10 10
20
15
10
21 20 17 21 20 21 21 21 8 16 7 15 30 33 64 33 34 34 35 33 36 64 33
14
13
8
25
25
19
18 7 17 6 164’ 5 6 17 18 6 17 6 6 17 6 16 10 12 20 23 10 6. 20 21 38 38 14 9 15 9 15 9 15 9 15 9 14 9 15 9 15 10 15 9 14 9
25
25
20
20
25
17
17 47 1S 46 1542 3943 19 49 18 46 19 48 19 45 18 47 13 29 26 56 12 28 25 56 52 112 9 39 9 40 9 139 9 '40 9 39 10 39 10 38 9 38 9 39 9 39
31
28
22
-
1 1’9 151 2 45'
0 0 0 0
7
5
5
18 17 14 17 17 17 17 17 15 30 16 3'2 63 11 11 11 11 11 11 11 11 11 11
6 ss2 5 9 6 6 6 6 6 6 6 6 6 6
15
17
15
6 6 5 6 6 6 6 5 3
8
6
5
8 17 4 4 4 4 4 4 4 4 5 5
6 7 6 7 7 7 7 6 4347 434-
14
13
5
6 6 5 6 6 6 6 7
4
7
5
6 10 6 6 6 6 5 5 5 5 6 6
4252
8
20
22
--
27 3 22 344' 30 3444 344' 33'7
Table
1 30s3 1 -M 1 25% 1 A5 1 2553 1 2P 1 2455a 1 2gS3 1 --XJ
4 -
7-
3 3 2 4 3 4 4 3 7-
-
8 -
4-
6-
10
914 -18 28 9 4----L39 4 9 4 9 4 9 4 9 4 9 4 9 4 9 4 9 4
814
812 10 12 8 10 10 12 10 12 10 12 10 12 10 11
9
12
716
44 44 45 46 44 46 46 47 48 49 48 49 49 50 51 52 53 52 53 53 53 51 52
44
42
41
41
continued
24 24 24 24 24 24 24 24 24
-
28 29 24 30 29 30 30 29 -48 -48
34
-4o
10
25
69c. 70a. 70b. 70~. 71a. 71b. 7lc. 71d. 72. 73. 74. 75. 76. 77. 78~ 78b. 78~. 79. 80a. 80b. 81. 82a. 82b.
acid
p-Casein B p-Casein B-l pCasein B-2 &Casein B, p-Casein C p-Casein C &Casein C &Casein C &Casein D +hsein A2 r-Casein B K-Casein dhsein &asein A t&asein A-l t&hsein A-2 &asein A-4 &asein B &h&n B-l K-Casein B-2 para-&asein para+Casein pat-a-&asein
Amino
A A
56S 5 5 5 556 555 5 5 555 5= 5= 5 3 4 3 4 3 4 3 2 2 3 4
5 5 5 6 5 7 5 5 7 6 6 18 13 20 74 14 14 21 14 14 10 14 13
.._~ --.
19 19 19 17 18 19 18 20 63 20 20 13 10 16 75 11 11 16 11 10 7 9 9
_ ~~..
6o 21 22 20 21 21 21 22 20 23 23 14 9 7o 8 8 77 7o 8 8 8 11 12
10 10 10 10 10 11 10 10 10 8 8 14 12 17 11 76 11 18 12 12 7 10 9 69
33 35 5a 33 34 34 L4 54 41 40 23 18 27 20 20 21 28 20 20 13 18 18
14 14 14 15 15 15 15 15 16 13 12 18 11 6* 73 14 11 68 73 12 8 11 10
TABLE
9 9 9 10 9 10 9 9 11 10 10 17 12 67 14 15 15 67 13 13 5 6 5
9 9 9 S6 9 10 9 9 10 9 9 17 11 17 12 16 12 16 11 11 8 11 12 27 27 18 27 27
99
38 40 40 Vi 37 62 38 39 57 39 39 36 25 69 27 27 26
2 (Continued)
-
2 2 2 2 2 2
179
179
1 2 2 2
6 6 6 5 6 6 5 6 5 7 7 2 2 3 2 2 2 3 2 2 1 1 1
11 11 11 11 12 12 12 12 12 12 12 12 9 13 9 9 9 13 9 9 7 9 9
5 5 5 5 4 4 4 4 4 3 4 7 5 8 5 5 78 8 5 5 5 8 7
6 9 6 9 6 9 6 9 6 9 6 9 6 9 6 9 5 8 6 11 7 11 3 8 3 4 7* 6 3 4 3 4 3 4 ‘1 6 3 4 3 4 3 4 4 6 4 6
4 4 4 4 3 5 4 4 4 5 5 13 9 13 8 8 8 13 8 8 9 13 13 -2 3
1 1 1 1 1 1 1 1 1 1 1 a6 2 2 2 2-2-2 2 2--
25 26
25 -
2Ssa 30s3 64 66 66 17 2672 -
1153 245a 25= 4.3 61 91
19
19
24 24 24 25 25 26 20
23
24 24
20 20
-
-
-
-
-
-
54 53 53 54 52 54 53 51 54 52 52 55 56 57 58 58 58 57 58 58 56 59 59
82~. para-r-Casein A 83a. para-&asein B 83b. para-r-Casein B 83~. para-r-Casein B 84. Catalase 85. Catalase 86. Catalase 87. Cellulase 88a. Ceruloplasmin I 88b. Ceruloplasmin IIa 88~. Ceruloplasmin IIb 88d. Ceruloplasmin IIIb 88e. Ceruloplasmin 89a. Ceruloplasmin, component I 89b. Ceruloplasmin, component II 90a. Ceruloplasmin I 90b. Ceruloplasmin II 91. Chloroperoxidase 92. Chlorophyll a-Protein 93. Chloroplast coupling factor 94. Chloroplast fraction I protein 95a. Chorismate mutase-prephenate dehydrogenase
67 85
89
48 49 12 19
18
18
50
56 65
64
62 66 24 30
2391
18
80
85 94
100
93 93 14 34
21
20
58
5 9 9 5 141 156 148 24 64 66 70 67
9 14 13 9 154 157 169 38 55 56 55 57
1 3 3 1 155 154 149 46 84 86 85 86
69
19
24
87 87 20 35
89
79 90
780 12 12 780 154 162 137 26 70 78 77 80
35
10
17
28 25 9 20
64
34
12
10
66 69 23 15
79
56 57 a7 77
613 10 19 9 18 613 79 166 85 167 84 176 14 25 53 54 55 55 58 54 60 52
36
11
15
84 87 33 17
91
69 93
7 11 10 7 97 104 105 39 73 68 66 66
36
14
18
74 75 17 16
92
86 92
3 6 6 3 96 107 108 41 88 87 83 87
69
18
19
150 154 39 26
165
135 136
7 11 11 7 294 266 286 53 143 136 137 137
82
21
35
160 170 26 24
134
130 145
18 27 27 18 197 213 231 32 133 131 133 129
-
-
-
8
4
1
2 1
-
17
4
7
26 23 2 4
15@ 26 25
2 2
1 2 2 1 29 41 44 208’ 52 14 4 13 26 15 27 12 26 15 20
-
34
12
11
82 84 4 9
92
68 83
7 9 10 7 116 126 121 19 70 71 70 72
41
10
16
33 33 6 11
44
46 46
5 7 7 5 130 121 126 17 43 44 44 42
16
6
2
39 37 7 15
42
43 43
27
10
7
58 51 13 21
83
54 71
3 4 4 6 5 6 3 4 89 132 70 120 81 128 7 16 44 55 45 55 44 56 46 58
20
9
7
56 54 10 8
76
71 71
9 13 12 9 86 80 80 19 68 71 69 310 -a -s3 -4 -a5
-33 16 -
--
--
8 -
20 20
-
-
71
70
69
67 67 68 16
66
65 66
60 59 59 60 61 61 62 63 64 64 64 64
continued
76
24
160 160 298V 33
162%
160 16Za8
250 250 256 49 160 160 160 160
Table
30z 16
3 -N
-
19 150
27 20 273
24 24
2 2
--
103d.
103~.
103b.
97. 98. 99a. 99b. 100. 101. 102. 103a.
96.
95c.
95b.
Chorismate mutase-prephenate dehydrogenase Chorismate mutase-prephenate dehydrogenase Chromaffin granule protein Chymopapain B Chymosin Chymotrypsin C, Chymotrypsin C Chymotrypsin II Chymotrypsin Chymotrypsin Chymotrypsinogen A Chymotrypsinogen B Chymokypsinogen C Chymotrypsinogen C
30
m
22
41 25 27 25 25 21 22 105
52
60
62
18
15
22
23
23
24
22
109 108
26 16 ‘07 18
16 19 21 19 18g6 21
50
17 21
25
55
72
27 21 23 19 22 20
51
81
73
20 13 93 12 24 97
54
86
14
15 15
14 12 15 12 15 100
68
33
37
5
15
14 111
11
12 10
13 15 14 21 11 11
7
39
38
26
“2
28
19 23
24 27 22 20 21 101
55
34
38
TABLE
17
17
17
18 19
17 18 16 14 19 102
19
37
39
32
2. 5
20
23 20
29 30 259” 22 23 9s
56
73
74
30
2s
26
15
21 16
30 29 25 21 18
156
87
87
2 (Coontinued)
10
10
10
10 10
11 6 10 7 8 g104
3
8
8
57
35
36
1
1
2
3 2
9
7
6
13 11
1 27 7 8 1 7 1 7 2 16 1’0.3 99
13
18
18
9
9
8
10 5 8 7 8473 7 3 5
42
44
41
6
6
3
t5 3 2
5 4 6 5
13
17
17
6
4
8
3 7 106
7 14 4 4
11
25
28
8
6
4
8 3 5
20 15 6 6
8
19
21
14
12-
13-
6 4 12 8 5-7 68
-
16
14
29 31
70
24
-
-
7 -
9 -
32
29
26
26 25 25
24
Q6
35 31
77
82
82
77
82
82
74 75 76 77 78 79 80 81
73
72
72
Chymotrypsinogen Chymotrypsinogen A Chymotryp sinogen A Chymotrypsinogen B Chymotrypsinogen B Chymotrypsinogen B Cocoonase Cocoonase
22 26
16 16
20 19
25
23
23
24
23
23
24
23
23 22
22
22
23 22
22
23
21 22
12 15
19
19
19
19
11 19
12 14
9
8
9
10
10 10
9 10
13
15
13
9
14 9
23 18
22
22
21
25
21 29
4 6 2
119
13 12
11
11
11
4 4
14
10 13
2
4 2
10116 4
10
10
10”s
8 10
7
7
4 5 4120 4
2
5
7
6 9
2
5
G
2
2
4
3 6
5
4 2
7 4
9 9
3
3
3
4
6 4
I4 63 residues of hydroxylysine. 15 No corrections for losses during hydrolysis, I6 Threonine and methionine sulphone. 17 30-31 residues. r8 13-14 residues. I9 11-12 residues. r0 13-14 residues. 21 8-9 residues. 22 16-17 residues. 23 28-29 moles. 24 26 moles (alkaline hydrolysis). 25 Number of residues based on assumption glycine. 28 22 moles by alkaline hydrolysis. 27 One Zn atom/mole. 28 24 moles by alkaline hydrolysis.
15 14
26 23
16 15
19
20117 18”8
20
22
19
15r1”
13 15
23
20
23’13
23 20
20 22
14 22
1 11-12 residues. la - not determined. z 2-3 residues. 3 Fifteen mole y0 N&; one manganese atom; l-2 glucosamine per molecular weight. 4 One mole FAD/50,000 g. 6 Three glucosamine per mole. GEleven glucosamine per mole, 19-12 cysteine residues, 3-4 cystine residues. r One cystine residue. 8 Values for residues normalized to make alanine = 15. No corrections for partial destruction of amino acids. 9 4-5 residues. 10 5-6 residues. r1 2-3 residues. r2 5-6 residues. 13 130 residues of 4-hydroxyproline.
107~ 107b.
106~.
106a. ) bb 106b.
105b.
‘r104. 105a.
16
18
16
21
23 24
26
26
25
26
25 25
Table
89 90
88
87
86
of
85’16
83 84
continued
of 16 residues
3 27 2 -
8
8
6
5
12 20 7-
28 Number of residues based on assumption of 22 residues of alanine. “Number of residues based on assumption of 3 residues of methionine. 81 Number of residues based on assumption of 17 residues of alanine. QNumber of residues based on assumption of 19 residues of alanine. 33 Two residues of amino sugar, 19 of hexose and 3 of fucose. 34 44 residues of hexose, 2 of fucose and no ammo sugar. H Five residues of amino sugar, 15 of hexose and 2 of fucose. 88 Six residues of ammo sugar, 17 of hexose, 2 of fucose. 37 The number of residues based on 81.3% recovery of weighed out sample. 38 The number of residues based on 99% recovery of weighed out sample (Ref 40, footnote d of Table 1) actually correspond to 95% recovery. 89 Two residues of amino sugar, 8 of hexose and 2 of fucose. 40 Results based on glycine to alanine ratio of 22:22 per molecule. 41 Eight residues of serine phosphate. (2 Eight residues of asparagine. W 14 residues of glutamine. u 12 phosphate groups. u 43-49 residues. (6 11-12 residues. 4r 11 phosphate groups. 48 Number of residues based on assumption of 4 residues of
TABLE arginine. 48 Uncorrected for decomposition; 1 disulfide 34,000 molecular weight. 6o 10-11 residues. s1 Uncorrected for decomposition. b* 2-3 residues. b3 Five atoms phosphorus. M 33-34 residues. SKWhole number residues per molecule containing 66 9-10 residues. 67 36-37 residues. 68 32-33 residues. 69 32-35 residues. m 21-22 residues. 61 Four atoms phosphorus. 62 38-39 residues. 63 17-18 residues. M 3-4 atoms phosphorus. 65 One atom phosphorus, 1 mole hexose. 66 l-2 residues. 67 20-21 residues. 68 18-19 residues. 69 3940 residues. r0 12-13 residues. ‘I 4-5 residues. 72 l-2 atoms phosphate. ‘3 12-13 residues. r4 13-14 residues.
2 (Continued)
5 glycine.
group
per
2
3
.Ej: w 3 z x
76 10-11 residues. 7q 11-12 residues. 77 8-Q residues. 78 4-5 residues. 79 True value believed to be 2 residues. 80 Each value adjusted so that value for leucine was 7. 81 Eight residues cysteine, 6 residues cystine. 82 32 moles mannose, 18 moles galactose, 3 moles fucose, 11 moles sialic acid, 16 moles hexoseamine, 28 moles glucoseamine. 83 17 moles mannose, 12 moles galactose, 1 mole fucose, 7 moles sialic acid, 10 moles hexoseamine. 84 20 moles mannose, 11 moles galactose, 2 moles fucose, 6 moles sialic acid, 17 moles hexoseamine, 9 moles glucoseamine. 86 23 moles mannose, 15 moles galactose, 3 moles fucose, 9 moles sialic acid, 17 moles hexoseamine, 9 moles glucoseamine. 86 One residue cysteine and 7 residues cystine. 8’ 57-64 residues. 8* 3% carbohydrate. 89 Without tryptophan, plus hemin. 90 4-5 chlorophyll a per mole; 1 mole carotenoid per 14 moles chlorophyll a. 91 All values normalized to 23 residues alanine. Q2 Based on 3 moles of tryptophan. 83 13-14 residues. Q4 All asparagine residues. 85 28,000-29,000.
w
0
$ F $ F;3
% u
3
116 Five cystine residues. 1x6 Calculated from sequence. 117 Seven asparagine residues. 11s Ten glutamine residues. 110 l-2 residues. 120 Amino acid analysis based residues.
111 13-14
on
assumption
of 4 histidine
E
8 %
of
112 22-23 residues. 113 11 asparagine residues. 114 10 glutamine residues.
mole
E
!?
per
of 18 leucine
residues.
96 Number of residues based on an assumed value residues. 97 16-17 residues. 98 20-21 residues. @g5-6 residues. 100 9-10 residues. 101 32-33 residues. 102 18-19 residues. 103Number of residues based on one methionine enzyme. lo4 Seven residues of cysteic acid formed. 10420-21 residues. 106 5-6 residues. IO7 23-24 residues. 108 16-17 residues. 109 24-25 residues. 110 26-27 residues.
252
DONALD
M.
KIRSCHENBAUM
ACKNOWLEDGMENTS I should like to express my thanks to the Marine Biological Laboratory, Woods Hole, Mass. for the use of their excellent library facilities during July and August, 1971 and July and August, 1972. The Library of the Downstate Medical Center, College of Medicine, has always been the prime source for the data compiled in this series of papers. I should like to thank the staff for their assistance. REFERENCES 1. 2. 3. 4.
FOR
TEXT
KIRSCHENRAUM, D. M. (1971) Anal. Biochem. 44, 159. KII(SCHENBAUM, D. M. (1972) Anal. Biochem. 49, 248. SPENCER, R. L., AND WOLD, F. (1969) Anal. Biochem. 32, 185. TANIS, R. J., TASHIAN, R. E, AND Yu, Y. S. L. (1970) J. Biol. REFERENCES
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