A compilation of amino acid analyses of proteins

A compilation of amino acid analyses of proteins

ANALYflCAL BIOCHEMISTRY A Compilation IX. 8, 466-499 ($975) of Amino Residues Hemoglobin, per Acid Mole Part Analyses of Protein A- of Protei...

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ANALYflCAL

BIOCHEMISTRY

A Compilation IX.

8,

466-499 ($975)

of Amino Residues Hemoglobin,

per

Acid Mole Part

Analyses of Protein A-

of Proteins -7.

Human

DONALD M. KIRSCHENBAUM Department

of Biochemistry, Brooklyn.

Downstate New, York

Medical 11203

Centrr-S

UN Y.

Received October 78, 1974; accepted December 1 I. 1974

In this compilation of data only one major group of proteins is listed, the hemoglobins of human origin (1). The first six amino acid analyses. Nos. 1-6, are the six individual chains, a. /3, y, S, E, and 5 chains. Tetramers of some of these chains have been reported and their individual amino acid compositions are easily obtained by multiplying the values of each of the individual chains by 4. The amino acid composition of normal, adult human hemoglobin is given in Table 2, No. 7 for comparison purposes. The amino acid composition of other normal human hemoglobins can be easily determined from the compositional data of the individual chains (Table 2, Nos. i-6). Beginning with No. 7 of Table 1 the listing is alphabetical with respect to the name given to the hemoglobin and not the type of hemoglobin, e.g.. No. 14 Hemoglobin N Akita is listed under A and not N, except for the Lepore and “anti” Lepore types which are at the end of the listing. All of the variants listed were detected by fingerprinting a tryptic peptide hydrolysate. The abnormal peptide was isolated and its amino acid composition determined or inferred. Table 1 lists the hemoglobin chains and hemoglobin mutants including the location of the mutation. Table 2 gives the compositional analysis of each tetrameric hemoglobin in residues of amino acid per mole (4 chains), except for nos. 1-6 where the data are given for the monomeric chain.’ Values for amino acid content which are different from that found in normal adult human hemoglobin. No. 7, are given in bold type. Part B of this series will be the amino acid composition of hemoglobins of nonhuman origin.’ ’ The analysis of No. 5, the e chain of hemoglobin U. or uterine hemoglobin (3) is given as percentages. L’Kirschenbaum. D. M., Anal. Bioclwrn.. to appear. 466 Copyrkht 0 1975 by Academic Press, Inc. All rights of reproduction in any form reserved.

AMINO

ACID

ANALYSES

OF

PROTEINS.

467

IX

ACKNOWLEDGMENTS The prime source of data is the Library of the Downstate Medical Center and I thank the librarians for their pleasant and very necessary assistance. A secondary source of data is the Library of the Marine Biological Laboratory. Woods l?ole, Mass., where I spent the summer months of 1973-1974 as a Library Reader. I thank the librarians of this very useful library for their assistance. I also thank Miss Margo Cohndreler for typing this manuscript and Mr. Edward Becker for checking the references.

REFERENCES 1. The previous published Bi~c~le~z.

paper in this series is Kil-schenbaum,

2. Szelenyi. J. G., and Hollan. S. R. (1969) Acta 47.

D. M. (1974)

Artal.

61, 567. Bioc~hinr.

Bioplrw.

Acrtd.

Sci.

Hrtng.

4,

468

DONALD

M. KIRSCHENBAUM TABLE 1 PROTEIN INDEX”

Number 1 2 3 4 5 6 7 7a 8 9 IO 11 12 13 14 15 16 17 18 19 20 21 2la 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 38a 39 40 41 42

Name Hemoglobin, Hemoglobin. Hemoglobin. Hemoglobin, Hemoglobin, Hemoglobin, Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin

a! chain fl chain y chain 6 chain E chain 5 chain A, a& A;, 616 J Abidjan, a5 1 Abraham Lincoln, /332 Abruzzo, p I43 G Accra, /379 Agenogi. fi90 Aida, a64 M Akita. p92 F Alexandra, ~12 Ankara. p IO Ann Arbor, 0180 0 Arab, /312 1 M Arhus. @63 Atago. (~8.5 G Audhali, (~23 G Azakouli, a68 Babinga, 6 I36 D Baltimore, (~68 J Baltimore, /3 16 N Baltimore. /395 J Bangkok. ,%6 Bethesda, /3 145 Beograd. p I2 I Bibba, a 13 6 Boras, PSS M Boston, ~~58 Brigham, @100 Bristol, 067 G Bristol, a68 J Broussais, (r90 D Bushman, p 16 Bucuresti p42 J Buda. a61 l Burlington, a 16 C, p6 J Cambridge, p69 Camden, j3 13 1 K Cameron, /3129

Number 43 44 45 46 47 48 49 50 51 52 53 54 54a 55 56 56a 57 58 59 60 61 62 63 64 6.5

66 67 68 69 70 71 72 ??a 73 74 75 76 77 78 79 80

81 82 83 84

Name Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemogiobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin

J Capetown, o92 Casper, ,BIO6 Chad, ~~23 Chesapeake, (r92 Chiapas, LYI14 D Chicago, PI 21 M Chicago, p63 G Chinese, (~30 Christchurch, p71 D Conley. p I2 1 G Copenhagen, /347 G Coushatta, p22 Creteil, PSS D Cyprus. /3 12 I Dakar, OLI I 2 Deer Lodge. /32 Denmark Hill. (r95 Dhofar, /358 F Dickinson, 797 Duarte, /362 E, p26 Edmonton. /t50 M Emory, p63 Etobicoke. (~84 Fx. ~136 L Ferrera, cu47 A, Flatbush. 822 Fort Worth, a27 Freiburg, p23 deleted G Galveston, /343 Genova, /328 G Georgia, (~95 M Gothenburg, n58 Gun Hill, @91-95 deleted J Habana, a7 1 M Hamburg. /363 Hammersmith, p43 C Harlem, p6873 Hasharon. 0147 Heathrow, 8103 1 High Wycombe, /359 Hijiyama, p I20 Hikari, 661 Hikoshima, (~54 Hirose. p37

AMINO

ACID

ANALYSES

TABLE

Number 85

86 87 88 89 90 91 92 93 94 95 96 97 97a 98 99 100 101 102 103 104 105 106 107 108 109 110 111 112 112a 113 114 115 116 117 118 119 120 121 122 123 124 135 126 127

Name Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin deleted Hemoglobin

OF

PROTEINS.

IX

469

I (Continued)

Number

Hiroshima, p 146 Hofu, /3 126 G Honan, p7 G Hong Kong, 0130 G Honolulu, a30 Hope, p 13 6 Hopkins I. /3Y5 Hopkins 2, cx112 G Hsi-Tsou. /379 G Hsin-Chu, 022 F Hull, 712 1 M Hyde Park, /392 I, ollh’ I1. al 6 D Ibadan, 087 K Ibadan. p46 Q India. a64 AZ Indonesia, 669 0 Indonesia. oil 16 I Interlaken, (~16 D Iran, p22 J Iran. p77 Q Iran. 0175 J Ireland, pl6 Istanbul. p92 M Iwate. 0187 F Jamaica. yhl Jenkins, p9S Kagoshima. (~57 M Kankakee, (~87 Kansas. /3102 J Kaohsiung, 059 Kempsey, /39Y Kenwood. p9S Khartoum, p 124 M Kiskunhalas, (~58 Knoxville I, a68 Koellicker, (Y14 1 Kobura, (~47 Koln. p98 J Korat. 056 Korle-Bu. p73 M Kurume, p63 Leiden, p6 or p7

1’8 128a 129 130 131 132 133 134 135 136 137 138 138a 139 140 141 142 143 144 145 146 147 148 149 14Ya I50 151 152 153 154 155 156 157 158 159 160 161 162 163 164 165 166 I67 168 I69

Little Rock, p 143

I693

Name Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin

D Los Angeles, p I2 1 Lyon, p 17-l 8 deleted Mahidol. 0174 G Makassar, /36 F Malaysia, ~136 Malmo, p97 F Malta. yl 17 J Manado. p56 Manitoba, (Y102 J Medellin, o22 J Meerut. cut20 J Meinung. 056 A, Melbourne, 643 Memphis. o23 N Memphis, p95 Mexico, cu54 M Milwaukee 1, /367 Moscva. /324 Nagasaki. p 17 N New Haven 2, p16 New York, PI 13 Nishiki 1, 0157 Norfolk, (~57 G Norfolk. (~85 Nottingham. /398 J Nyanza. a2 I N. Y. U., 812 Oak Ridge, pY4” Ocho Rios, 052 M Oldenberg, a87 Olmsted. p 14 1 Olympia, p20 D Ouled Rabah. 0 19 M Osaka, ~58 Osu Christiansborg, p52 J Oxford. 0115 P. @I 17 G Paris. (~64 J Paris 1, 0113 J Paris 2. a54 L Persian Gulf, a57 Perth, /332 G Pest. cu74 Peterborough, PI 1 I G Philadelphia, (~68 I Philadelphia, cul6

470

DONALD

M. TABLE

Number 170 171 172 173 174 175 176 177 178 179 180 181 182 183 184 185 186 187

Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin leted 188 Hemoglobin 189 Hemoglobin 190 Hemoglobin 191 Hemoglobin 19la Hemoglobin 191 b Hemoglobin 192 Hemoglobin 193 Hemoglobin 193a Hemoglobin 194 Hemoglobin 194a Hemoglobin 195 Hemoglobin 196 Hemoglobin 197 Hemoglobin 198 Hemoglobin 199 Hemoglobin 200 Hemoglobin 201 Hemoglobin 201 Hemoglobin 203 Hemoglobin 203a Hemoglobin 204 Hemoglobin 205 Hemoglobin 306 Hemoglobin 207 Hemoglobin 208 Hemoglobin 209 Hemoglobin

Name Philly. p35 G Port Arthur, /343 Porto Alegre. p9 D Portugal. p 12 1 D Punjab, p 12 1 M Radom, p63 J Rajappen, (~90 Rainier, /3 145 J Rambam. p69 Rampa, (~95 Richmond, p 102 Riverdale-Bronx, p24 J Rovigo, cu53 Rush, plO1 Russ. cu5 1 S. p6 Sabine, p91 St. Antoine, /374-75 deSt. Etienne, p92 St. Louis. /328 D St. Louis, 0168 St. Lukes. cu95 San Diego, p IO9 C San Jose, p7 Santa Ana. p88 J Sardegna, 0150 E Saskatoon, p32 G Saskatoon, p22 I Saskatoon, 0116 M Saskatoon, p63 Savannah, p24 Sawara, n6 Sealy, (~47 Seattle, p76 N Seattle, p61 Shepherds Bush, p74 Shimonoseki, (~54 J Sicilia. p65 Siam. al 5 Sinai, (~47 Singapore, a: 14 1 G Singapore, cu30 J Singapore, a78a79 Siriraj, /37 I Skamania. culh

KIRSCHENBAUM 1 (Continurd) Number 210 211 212 213 214 215 216 217 218 219 230 321 7,1 M-b 223 224 225 226 327 22x 229 230 231 232 233 234 235 236 237 238 239 240 341 242 243 244 245 246 247 248 249 250 251 252 253 254 255

Name Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin Hemoglobin

Sogn, /3 14 Southampton p 106 A, Sphakia, 62 Stanleyville 1, ~~68 Stanleyville 2, (~78 G ST1 , 0168 Sydney, p67 Szuhu, PSO Tacoma, p30 G Taegu. /322 Tagawa 1, n90 Tagawa 2. a47 G Taichung, a74 J Taichung, p 129 Taiwan-Ami, /325 Taipei, p22 Tak. p 147- 156 added Ta-Li. /383 F Texas I. y5 F Texas 2. y6 G Texas. /343 I Texas. al 6 D Thailand, /3 12 1 Q Thailand, ot74 Tochigi, /356-59 deleted Tokuchi, p2 J Tongariki, cul 15 J Toronto, ot5 Torino. a43 I Toulouse, p66 Tours. p87 deleted J Trinidad, /3 16 Ube 2, (~68 Umi, 0147 Uppsala, 0154 Waimanalo, (~64 D Washington. 0168 Wein. /3 130 Winnipeg, (~75 K Woolwich. p 132 X, cu68/36 Yakima, p99 Yoshizuka, p 108 Ypsi. /399 Yukuhashi, p58 Yukuhashi 2, (~47

AMINO

ACID

ANALYSES

TABLE

Number 256 257 25X 159 260 16 I

Name Hemoglobin Zambia, cu60 Hemoglobin Zurich, /363 Hemoglobin Lepore Augusta. l-876 I IS-l4q3 Hemoglobin Lepore Baltimore, l-50& 86-146@ Hemoglobin Lepore Boston, l-876, 11%1468 Hemoglobin Lepore Hollandia, 1-72s. 50-146#3

OF

PROTEINS.

IX

471

1 (forrtinrted)

Numher ‘h-2

263 264 265 266

-

Name Hemoglobin Lepore Pylas, I-87& 11%146/3 Hemoglobin Lepore Washington, l-87& 115-1468 Hemoglobin anti-Lepore Miyada, I-l?_@ 22-1466 Hemoglobin anti-Lepore P Nilotic. l-87/3, 116-1466 Hemoglobin Kenya l-807, 86-l46p

‘r No source is cited for the individual hemoglobins as all the hemoglobins are obtained from the same source-human erythrocytes. ’ A fetal type of hemoglobin I has been mentioned by Ranney rt al. (Ranney. H. M., O’Brien, C.. and Jacobs. A. S. (1962) NU~I~IYJ(Lorrrlon) 194. 743) and has the structure w,‘y,“. 5 Recent work (137a) has suggested that this is not a 94 replacement but is at 812 I.

acid

Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine ~et~onine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia Ref.

Amino

7 21 13 18 0 7 11 9 12 5 1 2 11 3 10 7 3 1 5’ 1a.b

1

13 15 18 18 0 7 5 7 13 11 2 1 11 3 9 8 3 2 92 lb

2

13 11 13 17 4 4 11 10 13 12 i 2 12 3 7 8 2 3 93 2

3

13 15 17 18 0 6 6 5 15 12 2 2 11 4 7 8 3 2 134 4

4

10 14 12 18 5 5 12 11 12 11 1 3 10 4 7 8 3 6

5

6

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 2g6 7

Residues

7 7a

index

38 72 60 72 0 26 34 28 54 34 6 8 44 16 34 30 12 6 368 7a

38 72 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 8

8 9

40 72 62 IO 0 30 32 32 50 32 6 6 44 12 38 30 12 6 28 9

of protein

numbers

OF PROTEIN

per molecule

Protein

TABLE 2 PER MOLECULE

4.1 8.4 8.6 12.6 1.7 -4.3 5.1 5.7 10.5 9.6 2.5 8.6 3.0 5.7 7.1 1.6 -5

5

RESIDUES

40 72 62 72 0 28 32 32 50 32 6 6 44 14 36 30 12 6 28 10

10

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 307 11

11

40 72 62 72 0 28 32 32 50 30 6 6 46 12 38 30 12 6 28 12

12

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 f2 6 30 13

13

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 14

14

-

-40 64 52 70 8 22 44 36 50 34 4 8 48 12 34 30 10 8 28 15

15

acid

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

Amino

40 IO 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 16

16

40 72 62 70 0 28 32 32 50 32 6 6 44 14 38 30 12 6 28 17

17

40 72 62 72 0 28 32 32 50 30 6 6 46 12 38 30 12 6 28 18

18

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 18

19

40 72 62 72 0 28 32 32 48 32 6 6 44 12 38 30 14 6 28 19

20

40 72 64 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 21

21

40 72 62 72 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 21a

Residues

21a

Protein

per 38 72 60 72 0 26 34 28 56 34 6 8 44 14 34 30 12 6 36 22

40 72 62 72 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 23

23

24

--

38 72 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 24

of protein

numbers

molecule

22

index

40 72 62 72 0 28 32 32 50 34 6 6 42 12 38 30 12 6 28 25

25

38 72 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 26

26

40 72 64 72 0 28 32 32 50 30 6 6 44 12 38 30 12

6 28 28

10

6 28 27

28

40 72 62 72 0 28 32 32 50 32 6 6 44 12 40 30

27

40 72 62 70 0 30 32 32 50 32 6 6 44 12 38 30 12 6 28 29

29

40 72 62 70 0 28 32 32 50 32 6 6 44 14 38 30 12 6 28 30

30

P .I 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 Ref.

Amino

40 12 62 74 0 26 32 32

50

32 6 6 44 12 38 30 12 6 28 32

50

32 6 6 44 12 36 30 14 6 28 31

32

40 72 62 72 0 28 32 32

31

40 72 60 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 33

33

40 72 62 72 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 34

34

40 72 62 72 0 28 32 32 52 32 6 6 42 12 38 30 12 6 30 35

35

40 72 62 74 0 28 32 32

50 32 6 6 44 12 38 28 12 6 28 37

50 32 6 6 44 14 38 30 12 6 28 36

Residues

37

Protein

40 72 62 72 0 28 32 32 52 32 6 6 42 12 38 30 12 6 30 38

39

34 6 6 42 12 38 30 12 6 28 38a

40 72 62 72 0 28 32 32 50 30 6 6 46 12 38 30 12 6 28 39

of protein

50

40 72 62 72 0 28 32 32

38a

numbers

per molecule

38

index

2 (Continued)

38 72 62 72 0 28 32 32

36

TABLE

38 72 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 40

40

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 26 41

41

40 70 62 72 0 28 32 32 -9 -9 6 6 44 12 38 30 12 6 28 42

42

40 72 62 72 0 28 32 32 50 34 6 6 44 10 38 30 12 6 30 43

43

40 72 62 70 0 30 32 32 50 32 6 6 44 12 38 30 12 6 28 44

44

30 6 6 46 12 38 30 12 6 28 45

50

40 72 62 72 0 28 32 32

45

acid

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

Amino

40 72 62 74 0 28 32 32 50 32 6 6 44 10 38 30 12 6 28 26

46

40 72 62 72 0 26 32 32 50 32 6 6 44 14 38 30 12 6 28 46

47

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 47

48

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 48

49

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 49

50

40 72 62 72 0 28 34 32 50 32 6 6 44 I? 38 28 12 6 28 50

51

40 72 62 12 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 47

Residues

52

Protein

40 72 62 12 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 40

40 74 62 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 51

54

54a

40 72 62 72 0 28 30 32 52 32 6 6 44 12 38 30 12 6 30 51a

of protein

numbers

per molecule

53

index

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 47

55

40 72 62 72 0 28 32 32 50 34 6 6 44 12 36 30 12 6 30 52 -

56

40 72 62 12 0 28 32 32 50 32 6 6 44 14 36 30 12 6 28 52a

56a

40 74 62 72 0 26 32 32 50 32 6 6 44 12 38 30 12 6 28 53

57

-

40 72 62 72 0 26 32 32 50 32 6 6 44 14 38 30 12 6 28 54

58

40 64 52 70 8 22 44 38 50 34 4 8 46 14 32 30 10 8 28 55

59

40 72 62 72 0 28 32 32 50 30 6 6 46 12 38 30 12 6 28 57

40 72 62 72 0 28 32 30 50 32 6 6 46 12 38 30 12 6 28 58

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 31

63

40 72 62 72 0 28 30 32 50 32 6 6 44 14 38 30 12 6 28 59

64

38 66 52 70 8 22 44 38 50 34 4 8 46 12 34 30 10 8 28 3

65

66

42 72 62 72 0 28 32 32 48 32 6 6 44 12 38 30 12 6 28 60

40 70 62 72 0 30 32 32 50 32 6 6 44 12 38 30 12 6 28 56

-

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

62 Residues

61

Protein

per 40 70 60 72 0 26 34 28 54 36 6 8 44 14 34 30 12 6 36 61

42 72 62 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 62

68

69

42 72 60 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 28 63

of protein -

numbers

molecule

67

index

2 (Confinrred)

acid

Amino

60

TABLE

42 74 62 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 64

70

42 72 62 70 0 30 32 32 50 32 6 6 44 12 38 30 12 6 28 65

71

42 72 62 74 0 26 32 32 50 32 6 6 44 12 38 30 12 6 28 66

72

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 66a

72a

42 72 62 70 0 28 32 32 48 32 4 6 42 12 36 30 12 6 28 67

73

40 70 62 72 0 28 32 32 50 34 6 6 44 12 38 30 12 6 28 68

74

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

Amino acid

69

28

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6

75

-

70

28 12 6 28

-

30 71

12 38 30 12 6

50 30 6 6 44

50

32 6 6 44 12 38

0

28 32 32

0

72

30 12 6 28

44 12 40

48 32 6 6

28 32 32

0

62 72

64 72

28 34 32

40 72

78

40 72

77

72 62 72

40

76

28 73

12 6

38 28

12

50 32 6 6 44

28 32 32

0

62 74

40 72

79

28 74

12 6

42 12 38 30

6

32 50 34 6

28 32

0

62 72

40 72

80

82

83

84

75

6 28

12

12 38 30

6 42

6

50 34

28 32 32

0

62 72

40 72

12 6 30 76

6 42 12 38 30

-

26 77

12 6

14 38 30

32 32 50 30 6 6 44

32 32 52 32 6

28

0

62 72

40 72

28

0

62 72

40 72

77

-

28

4

12

30

44 12 38

32 6 6

28 34 32 50

0

72 62 72

40

Residues per molecule of protein -

81

Protein index numbers

28 78

12 6

30

12 36

44

32 32 52 32 6 6

62 72 0 28

40 72

85

-

79

6 28

12

6 44 12 38 30

32 32 50 34 6

28

0

60 72

40 72

86

80

6 28

12

12 38 30

46

6

30 6

28 32 32 50

0

72 62 72

40

87

81

12 6 30

38 30

12

6 44

32 6

50

28 32 32

0

72 62 72

40

88

81

30 12 6 30

6 44 12 38

32 6

32 32 50

28

0

62 72

40 72

89

82

30 12 6 28

6 44 12 38

52 32 6

28 32 32

0

62 72

38 72

90

Ref.

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

Amino acid

40 72 62 72 0 28 32 32 50 34 6 6 42 12 38 30 12 6 28 83

91

40 72 62 72 0 28 32 32 52 32 6 6 44 12 36 30 12 6 28 84

92

42 72 62 72 0 28 32 32 48 32 6 6 44 12 38 30 12 6 28 85

93

40 74 62 72 0 28 32 32 so 30 6 6 44 12 38 30 12 6 28 86

94

40 64 52 70 8 22 44 38 50 32 4 8 48 12 34 30 10 8 28 87

95

-40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 88

96

40 72 62 72 0 28 32 32 SO 34 6 6 42 12 38 30 12 6 28 89

-.

97 9?d

-

98

Protein index numbers

2 K’onrinrted)

99

40 72 60 72 0 26 34 28 54 36 6 8 42 14 34 30 12 6 36 38~1

40 72 62 72 0 28 32 30 50 32 6 6 46 12 38 30 12 6 28 90

38 72 62 72 0 28 32 32 50 34 6 6 44 12 38 30 12 6 28 42

Residues per molecule of protein

-

TABLE

40 72 62 72 0 28 32 32 48 32 6 6 44 12 40 30 12 6 28 91

100

38 72 60 72 0 26 34 28 54 34 6 8 44 16 34 30 I2 6 36 92

_- -~

101

40 72 62 72 0 28 32 32 50 30 6 6 46 12 38 30 12 6 28 93

102

38 72 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 94

103

40 72 62 72 0 28 32 32 SO 32 6 6 44 12 38 30 12 6 30 95

104

40 72 62 72 0 28 32 32 52 32 6 6 44 12 36 30 12 6 28 96

105

479

acid

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

Amino

42 72 62 72 0 28 32 32 48 32 6 6 44 12 38 30 12 6 28 111

121

40 72 60 72 0 28 32 32 50 32 6 8 44 12 38 30 12 6 28 112

122

38 72 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 113

123

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 114

124

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 115

125

40 72 62 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 116

126

TABLE

40 72 62 72 0 28 32 32 50 34 6 6 44 12 36 30 12 6 30 117

Residues

127

Protein

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 47

129

40 72 60 72 0 28 32 32 50 32 6 6 42 12 38 30 12 6 28 117a

40 72 62 72 0 28 32 32 48 32 6 6 44 12 40 30 12 6 28 118

of protein

128a

numbers

per molecule

128

index

2 (Continued)

40 74 62 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 119

130

38 64 52 70 8 22 44 38 50 34 6 8 46 12 34 30 10 8 28 120

131

40 72 62 72 0 28 32 32 50 34 6 6 44 12 36 30 12 6 30 121

132

40 64 52 70 8 22 44 38 50 34 4 8 46 14 32 30 10 8 28 122

133

38 72 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 123

134

40 72 62 72 0 28 30 32 50 32 6 6 44 10 38 30 12 6 28 124

135

PP 9 9 Zf 2s SE Zf 85. 0 ZL z9 ZL 8C

WI

6PI

e6PI

ZI

PEI 82 9 51 Of 8f

SE1 OE 9 ZI Of 8E ZI PP 9 9 Zf OS Zf ZE 82. 0 ZL z9 ZL OP

YEI 82 9 21 Of 8f ZI PP 9 9 Zf OS Zf Zf 82 0 ZL 09 ZL zv

LPI

rrLL 85 9 ZI Of 8f ZI PP 9 9 Zf 2s Zf Zf 82 0 ZL z9 ZL 8E

YPl

PP 9 9 DE OS zc Zf 8Z 0 ZL 09 ZL OP

ZI

EEI 82 9 ZI Of 8f

S-PI

PP 9 9 Zf zs Zf Zf 82 0 ZL 59 ZL SE

ZI

ZEI 82 9 zr Of 8f ZI VP 9 9 Zf ZS Zf Zf 82. 0 ZL z9 ZL 8E

ZI Of 8E

OEI 82 9

IE 82 9 ZI Of 8E ZI Pp 9 9 PE OS Zf Zf 82. 0 ZL 09 ZL OP

621 9Z 9 ZI Of 8f ZI PP 9 9 ZE OS Zf SE 82 0 ZL z9 ZL OP

Pt‘I SlaqUInU

EPI

XapU!

ZPI UyOld

IPI

u!alold JO aItma[om lad sanp!sax

IZI 82 9 51 Of 8f ZI ZP 9 9 PE OS Zf Zf 82 0 ZL z9 ZL OP

OtrI

821 01-9 ZI Of 8f ZI ZP 9 9 PE OS SE Zf 82 0 ZL z9 ZL OP

6fI

951 82. 9 ZI

Of SE

Of 8f

QEI

9z 0 ZL 09 ZL OP

8fI

LEI

9fI

ZL Z9 ZL SE

ZL z9 OL OP

ZL 59 ZL 8E

Zf Zf 82 0

ZS

ZE zs ZE Zf 82 0

PE OS zt Zf 82 0 SE

Zf PS 8Z Pf

ZI Pf 9 9

9f 8f

551 82 9 51

ZI VP 9 9

ZI PP 9 9

82 9 ZI

CII

PI 9P 8 9

Pf

8E ZI PP 9 9 Zf OS SC Zf 8Z 0 ZL z9 ZL OP

ZI Of

e9ZI 9f 9 ZI Of

LZL OC 9

‘33x

p!x OU!uJV

p’x 3!unz~tl~~ p!x qnzdsv au!uoa.qL au!.rag auwd au!maIoq aqma7 auw au!uqv au!zKlg

EJU~S.h-JIl2H

au!uoglqq

ati@7

~younm ap!wv ueqdo$dhL au!so.htL au~uapqbuaqd aupls!H au~u!8Jv

acid

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

Amino

40 IQ 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 136

150

40 72 60 72 0 26 34 28 52 34 6 8 46 14 34 30 12 6 34’2 136a

151

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 137

152

40 74 62 72 0 28 32 32 48 32 6 6 44 12 38 30 12 6 28 138

153

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 139

154

40 12 62 70 0 28 32 32 50 32 6 6 44 14 38 30 12 6 28 121

155

TABLE

40 12 60 72 0 28 32 32 50 32 6 8 44 12 38 30 12 6 28 140

Residues

156

Protein

40 72 62 12 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 141

159

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 142

40 12 62 12 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 143

of protein

158

numbers

per molecule

157

index

2 (Continued)

38 72 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 144

160

40 72 62 12 0 28 32 32 50 32 6 6 44 14 36 30 12 6 28 145

161

40 72 62 72 0 28 32 32 48 I3 32 6 6 44 12 38 30 12 6 28 146

162

40 70 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 147

163

40 72 62 12 0 28 32 32 50 32 6 6 44 12 38 30 12 6 26 148

164

38 72 62 I? 0 28 32 32 50 32 6 6 44 14 38 30 12 6 28 149

165

40 12 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 151

40 72 60 72 0 28 32 32 50 32 6 6 44 12 38 32 12 6 28 152

40 72 62 12 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 153

-

40 72 62 72 0 28 32 32 50 34 6 6 42 12 38 30 12 6 28 89

169a

6 28 154

10

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 32

170 171

40 74 62 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 155

40 72 62 70 0 30 32 32 50 32 6 6 44 12 38 30 12 6 28 150

169

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

168 Residues

167

acid

Amino

166

Protein

40 72 62 72 0 28 31 I4 32 50 32 7 I4 6 44 12 38 30 I2 6 28 156

40 72 62 12 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 47

173

174

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 47

of protein

numbers

per molecule

172

index

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 157

175

40 72 62 72 0 28 32 34 50 32 6 6 42 12 38 30 12 6 28 158

176

-

40 72 62 72 0 28 32 32 50 32 8 6 44 12 38 30 10 6 28 21

177

38 72 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 159

178

40 72 62 72 0 26 34 32 50 32 6 6 44 12 38 30 12 6 28 160

179

40 72 62 72 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 161

180

40 70 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 163

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 164

38 72 62 72 0 28 32 32 50 32 6 6 44 14 38 30 12 6 28 165

40 72 64 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 166

185

40 72 62 70 0 30 32 32 50 32 6 6 44 12 38 30 12 6 28 167

186 187

38 72 62 70 0 28 32 32 50 32 6 6 44 12 38 30 12 6 28 168

38 72 62 72 0 28 32 32 50 32 6 6 44 14 38 30 12 6 28 162

184

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

183 Residues

182

Protein

40 72 62 72 0 28 32 32 50 34 6 6 44 12 36 38 12 6 30 169

40 72 62 70 0 28 32 32 50 34 6 6 44 12 38 30 12 6 30 170

189

190

40 72 62 72 0 28 32 32 50 30 6 6 46 12 38 30 12 6 26 21a

of protein

numbers

per molecule

188

index

2 (Continued)

acid

Amino

181

TABLE

40 72 62 72 0 26 32 32 50 32 6 6 44 14 38 30 12 6 28 171

191

40 72 60 72 0 28 32 32 50 32 6 8 44 12 38 30 12 6 28 171a

191a

38 72 62 72 0 28 32 32 50 34 6 6 44 12 38 30 12 6 28 171b

191b

40 12 62 70 0 30 32 32 50 32 6 6 44 12 38 30 12 6 28 172

192

40 72 62 72 0 28 32 32 52 32 6 6 44 12 36 30 12 6 28 173

193

40 72 62 72 0 28 32 32 50 30 6 6 46 12 38 30 12 6 28 173a

193a

P8I 92 9 21 Of 8E ZI PP 9 9 Zf OS ZE Zf 82 0 ZL Z9 OL m

LOZ

18 OE 9 ZI Of 8& ZI PP 9 9 ZE OS ZE Zf 82 0 ZL z9 ZL OP

9OZ

z9

LO1 82 9 21 Of 8E 01 tP 9 9 Zf OS Zf Zf OE 0 ZL ZL Oti

soz

-

Of OP ZI Pb

E81 82 9 ZI

9 9 Zf OS Zf ZE 82 0 ZL 19 ZL SC

Of 8f PI PP

VZSI 82 9 ZI

"fOZ

9 9 Zf 817 Zf Zf 82 0 ZL Z9 ZL OP

POZ

- -281 of 9 ZI Of 8E ZI ZP 9 9 Zf ZS Zf Zf 82 0 ZL z9 ZL OP

EOZ --

Of OS Zf Zf

181 92 9 ZI Of 8E PI PP 9 9

Zf zs Zf Zf

081 85 9 ZI Of 8E ZI m 9 9

PE OS Zf Zf

6LI 82 9 21 Of 8E ZI ZP 9 9

PE OS Zf Zf

8LI 82 9 ZI Of 8f ZI w 9 9

Zf SP Zf Zf

LLI 82 9 ZI Of 9C ZI # 9 9

ZE 89 Zf Zf

911 82 9 ZI Of 8E ZI PP 9 9

Zf OS Zf ZE

SLI 8Z 9 ZI Of 8f ZT # 9 9

85. 0 ZL Z9 ZL OP

Zf OS if Zf

IE 8Z 9 VI Of 9t ZI Pt 9 9

82 0 ZL z9 ZL OP

PC OS Zf Zf

eVL1 82 9 ZI Of 8E ZI ZP 9 9

82 0 ZL z9 PL OP

OE OS Zf Zf

VLI 82 9 ZI Of 8E ZI t-9 9 9

P61

8Z 0 ZL p9 ZL 8E

-

82 0 ZL z9 PL OP

V61

82 0 ZL z9 ZL OP

561

82 0 ZL z9 OL OP

~

961

82 0 zf. 29 ZL OP

661

L61

82 0 ZL z9 ZL SC

ooz

II;alOJd

861

82 0 ZL z9 ZL OP

IOZ

XapU!

u!a$o.rd 30 a[nzalou~ .~ad sanplsax zoz

S.I%+llllU

‘32x

epounue ap!mv ueqdoldr(q au!soJd;l au!uepqr(uayd au!pgs!H au!u@rv kXI!S&J auruoyayy augsl(3-3[qg p!se s!uIemlf) p!x q.mdsv au!uoa.q;l 3U!.q

aU!lO.Id

aurmaloq XpXXYJ =!@A auyuqv aupqf)

p!3e ou!my

acid

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

Amino

-

40 72 62 72 0 28 32 32 50 30 6 6 46 12 38 30 12 6 28 18.5

208

40 72 62 72 0 28 32 32 50 34 6 6 42 12 38 30 12 6 28 186

209

40 12 62 IQ 0 28 32 32 50 32 6 6 44 14 38 30 12 6 28 187

210

40 72 62 70 0 30 32 32 50 32 6 6 44 12 38 30 12 6 28 188

211

40 72 60 72 0 26 34 28 54 34 6 8 44 16 32 30 12 6 36 189

212

40 72 62 12 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 190

213

TABLE

40 72 62 72 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 191

Residues

214

215

index

40 72 62 12 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 192

40 74 60 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 28 193

216

217

40 72 62 72 0 28 32 32 48 32 6 6 46 12 38 30 12 6 26 194

of protein

numbers

per molecule

Protein

2 (Continued)

38 30 12 6 28 195

10

40 72 62 72 0 28 34 32 50 32 6 6 44

218

40 74 62 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 196

219

40 72 62 72 0 28 32 32 52 32 6 6 42 12 38 30 12 6 30 77

220

42 72 62 72 0 28 32 32 4.8 32 6 6 44 12 38 30 12 6 28 77

221

40 72 62 72 0 28 32 32 48 32 6 6 44 12 40 30 12 6 28 80

222

40 70 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 197

223

42 72 62 72 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 199

40 74 62 78 0 28 34 34 52 32 6 6 46 12 40 32 16 6 30 200

38 72 62 12 0 28 32 32 50 32 8 6 44 12 38 30 12 6 28 201

30 64 52 IO 8 22 44 38 50 32 4 8 48 12 34 30 10 8 28 202

228

30 64 52 70 8 22 44 38 50 32 4 8 48 12 34 30 10 8 28 203

229 230

40 74 62 12 0 28 32 32 50 30 6 6 44 12 38 30 12 6 28 155

38 72 62 72 0 28 32 32 50 32 6 6 44 14 38 30 12 6 28 198

227

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

226 Residues

225

acid

Amino

224

231

index

40 72 62 72 0 28 32 32 50 34 6 6 42 12 38 30 12 6 28 204

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 30 205

232 233

40 72 62 72 0 28 32 32 48 32 6 6 44 12 40 30 12 6 28 87

of protein

numbers

per molecule

Protein

38 72 62 72 0 26 32 32 48 32 6 6 42 12 38 30 12 6 26 206

234

40 72 62 72 0 28 32 32 50 32 6 6 44 12 36 30 14 6 28 201

235

40 70 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 208

236

40 70 62 72 0 28 32 32 52 32 6 6 44 12 38 30 12 6 28 209

237

40 72 64 72 0 28 32 32 50 32 6 6 44 12 38 28 12 6 28 210

238

40 72 62 72 0 28 32 32 50 34 6 6 42 12 38 30 12 6 28 211

239

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

Amino acid

-

40 72 62 72 0 28 32 30 50 32 6 6 44 12 38 30 12 6 28 168

--

-. 240

38 72 62 72 0 28 32 30 52 32 6 6 44 12 38 30 12 6 28 78

-

241

40 72 62 72 0 28 32 30 50 32 6 6 44 12 38 30 12 6 26 212

242

42 72 62 72 0 28 32 30 48 32 6 6 44 12 38 30 12 6 28 111

--

243

40 72 62 72 0 28 32 30 50 32 6 6 44 12 38 30 12 6 26 213

244

246

247

248

Protein index numbers

2 (Continued)

249

Residues per molecule of protein -. 40 40 40 40 40 72 72 72 72 72 62 62 62 62 62 72 72 72 72 72 0 0 0 0 0 28 28 28 28 28 32 32 32 32 32 30 32 32 32 32 50 48 52 48 50 32 32 32 32 34 6 6 6 6 6 6 6 6 6 6 44 46 44 44 42 12 12 12 12 12 38 38 38 38 38 30 30 30 30 30 12 12 10 14 12 6 6 6 6 6 30 26 28 28 30 214 215 216 217 42

245

TABLE

40 72 62 72 0 28 32 32 48 30 6 6 48 12 38 30 12 6 26 218

250

40 72 62 72 0 28 32 32 48 32 6 6 44 12 40 30 12 6 28 219

-

251

40 72 62 72 0 28 32 32 50 32 6 6 44 12 38 30 12 6 26 220

252

40 72 62 72 0 28 32 32 48 32 6 6 44 12 38 30 14 6 28 221

253

40 72 62 72 0 26 32 32 50 32 6 6 44 14 38 30 12 6 28 77

254

--

42 72 62 72 0 28 32 32 48 32 6 6 44 12 38 30 I2 6 28 77

25.5

acid

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

Amino

40 72 62 72 0 28 32 32 52 32 6 6 42 12 38 30 12 6 30 222

2.56

40 72 62 72 0 28 32 32 50 32 6 6 44 14 36 30 12 6 28 223

257

40 72 62 72 0 28 34 28 52 32 6 6 44 12 38 30 12 6 32 224

25s

40 74 62 72 0 28 32 30 52 30 6 6 44 12 38 30 12 6 26 225

259 261

index

40 74 62 72 0 28 30 32 52 30 6 6 44 12 38 30 12 6 30 227

263

40 72 62 72 0 28 34 28 52 32 6 6 44 12 38 30 12 6 32 224

of protein 40 72 66 72 0 28 34 28 52 32 6 6 44 12 38 30 I2 6 32 226

262

numbers

per molecule

22615

40 72 62 72 0 28 34 28 52 32 6 6 44 12 38 30 12 6 32

Residues

260

Protein

40 70 60 72 0 26 36 28 52 36 6 8 44 14 34 30 12 6 34 228

264

40 72 60 52 0 36 32 32 52 34 6 8 44 10 34 30 12 6 32 229

265

40 70 56 68 6 24 36 36 52 30 6 6 46 12 38 30 12 6 28 230a.b

266

r From sequence; the amide ammonia is distributed as 4 asparagine and 1 glutamine residues. There are 141 residues for a molecular weight of 15,126. 2 From sequence; the amide ammonia is distributed as 6 asparagine and 3 glutamine residues. There are 146 residues and the molecular weight is 15.867. 3 From sequence; the amide ammonia is distributed as 5 asparagine and 4 glutamine residues. There are two kinds of gamma chain--one chain has alanine at position 136 and the other chain has glycine at this position. The data are presented for the glycine-containing chain with 146 residues and the molecular weight is 15,995. 4 From sequence; the amide ammonia is distributed as 8 asparagine and 5 glutamine residues. There are 146 residues for a molecular weight of 15,924. 5 These values are percentages and are given so the user will have some data about ah the single chains of which the hemoglobins consist. 6 The amide nitrogen is distributed as 20 asparagine and 16 glutamine residues. ’ The amide nitrogen is distributed as 22 asparagine and 8 glutamine residues. Recently there was a report of Hemoglobin Munchhausen which is, of course, HbA, (Y& (76). s The amide nitrogen distributed as 24 asparagine and 12 glutamine residues. g Either glutamic acid or aspartic acid is the replacement (42). lo Either glutamic acid or glutamine is the replacement. If glutamine, then the amide content is increased to 30. I1 Hemoglobin Nishiki 2, o57, and hemoglobin Nishiki 3, ~~57 have also been reported with the same amino acid substitution (77). I2 The amide nitrogen is distributed as 18 asparagine and 16 glutamine residues. I3 The aspartic acid is replaced by some neutral amino acid, therefore, the number of residues for one of the amino acids is wrong. I4 Only one of the p chains has a change of cysteine for serine (156a). I5 Hemoglobin Lepore of French origin (226a) and of Iranian origin (226b) have been reported. Both are similar to the Boston variety (226a. 226b).

AMINO

ACID

ANALYSES

OF

PROTEINS.

IX

491

REFERENCES 1. (a) Hill, R. J., Konigsberg, W., Guidotti. G.. and Craig, L. C. (1962) J. Biol. C/rem. 231, 1549. (b) Braunitzer, G., Gehring-Muller, R., Hilschmann. N., Hilse, K.. Hobom, G.. Rudloff, V., and Wittman-Liebold, B. (1961) Hoppe’Seyler’s Z. Physiol. Chem. 325, 283. 2. Schroeder, W. A., Shelton, J. R., Shelton, J. B.. Cormick. J.. and Jones, R. T. (1963) Biochemistry

2, 992.

3. Schroeder, W. A., Huisman, T. H. J., Shelton, J. R., Shelton, J. B., Kliehauer, E. F., Dozy. A. M., and Robberson. B. (1968) Proc. Nut. Acad. Sci. USA 60, 537. 4. Jones, R. T. (1964) Cold Spring Harbor Symp. Quant. Biol. 29, 298. 5. Szelenyi, J. G.. and Hollan, S. R. (1969) Acta Biochim. Biophys. Acad. Sci. Hung. 4, 47. 6. Capp, G. C., Rigas, D. A.. and Jones, R. T. (1970) Nurure (London) 228, 278. 7. Jones, R. T., Schroeder. W. A., Balog, J. E.. and Vinograd. J. R. ( 1959) J. Amer. Chem.

Sot.

81, 3 161.

7a. Ball, E. W.. Meynell, M. J.. Beale, D.. Kynoch. P.. Lehmann, H., and Stretton. A. 0. W. (1966) Nature (London) 209, 1317. 7b. Lindenbaum, J. (1974) .I. Amer. Med. Assoc. 228, 498. 8. Cabannes, R.. Renaud, R.. Mauran, A.. Pennors, H., Charlesworth. D., Price, B. G., and Lehmann, H. ( 1972) Now. Rev. Fr. Hematol. 12, 289. 9. Honig, G. R.. Green. D., Shamsuddin. M.. Vida. L. N.. Mason, R. G., Gnarra, D. J., and Maurer. H. S. (1973) ./. Clin. Imvst. 52, 1746. 10. Tentori, L., Carta Sorcini, M., and Buccella. C. (1972) Clin. Chim. Acta 38, 258. 11. Lehmann, H.. Beale, D., and Boi-Doku, F. S. (1964) Nature (London) 203, 363. 12. Miyaji, T.. Suzuki, H., Ohba, Y., and Shibata, S. (1966) Clin. Chim. Acta 14, 624. 13. Ramot. B., Kinderlerer, J.. and Lehmann, H. (1972) cited in World Health Organ. Tech. Rep Ser. No. 509. ref. 127 on p. 52. 14. Miyaji. T., luchi, I., Karita, K.. Ohba, Y.. Yamamoto, K.. and Shibata, S. (1967) Bull. Yamaguchi Med. School 14, 18 1. 15. Loukopoulos, D., Kaltsoya. A., and Fessas, Ph. (1969) Blood 33, I 14. 16. Arcasoy. A.. Casey, R., Lehmann. H., Cavdar, A. O., and Berki, A. (1974) Fed. Eur. Biochem. Sot. Lett. 42, 121. 17. Adams, J. G., Winter. W. G., Rucknagel. D. L., and Spencer, H. H. (1970) BIood 36, 851. 18. Baglioni, C., and Lehmann, H. (1962) Nature (London) 196, 129. 19. Hobolth, N. (1965) Acta Paediat. Stand. 54, 357. 20. Fujiwara, N., Maekawa, T.. and Matsuda, G. (1971) Znt. 1. Protein Res. 3, 35. 21. Marengo-Rowe, A. J.. Beale, D.. and Lehmann. H. (1968) Natltre (London) 219, 1164. 21a. Baglioni, C. cited in Weatherall. D. J., Sigler, A. T.. and Baglioni, C. (1962) Bull. Johns

Hopkins

Hosp.

111,

143.

22. DeJong. W. W., and Bernini. L. F. (1968) Nature (London) 219, 1360. 23. Weatherall. D. J., Sigler, A. T., and Baghoni, C. (1962) Bull. Johns Hopkins

Hosp.

111, 143.

24. Baglioni, C., and Weatherall. D. J. (1963) Biochim. Biophys. Acta 78, 637. 25. Clegg. J. B., Naughton. M. A., and Weatherall, D. J. (1965) Nature (London) 207, 945. 26. Clegg, J. B., Naughton, M. A., and Weatherall. D. J. (1966) J. MO/. Biol. 19, 91. 27. Hayashi, A., Stamatoyannopoulos, G., Yoshida. A., and Adamson. J. (1971) Nature Nenj Biol. 230, 264.

492

DONALD

M. KIRSCHENBAUM

28. Efremov, G. D., Duma, H., Ruvidic. R., Rolovic, 2.. Wilson, J. B., and H&man, T. H. J. (1973) Biochim. Biophys. Actcr 328, 81. 29. Kleihauer, E. F., Reynolds, C. A., Dozy, A. M., Wilson. J. B.? Moores, R. R., Berenson, M. I’., Wright, C. S., and Huisman, T. H. J. (1968) Biochim. Biophys. Acta 154, 220. 30. Hollender, A., Lorkin, P. A., tehmann. H., and Svensson, B. (1969) Nature (London) 222, 953. 31. Gerald. P. S., and Efron. M. L. (1961) Proc. Nut. Acnd. Sci. 47, 1758. 31a. Baglioni, C.. and Ventruto, V. (1968) Ez~r. I. Bioehem. 5, 29. 32. Lokich, J. J., Moloney. W. C.. Bunn, H. F., Bruckheimer, S. M., and Ranney, H. M. (1973) J. Clin. Imvest. 52, 2060. 33. Steadman. J. II., Yates, A., and Huehns, E. R. (1970) Brit. J. Hematol. 18, 435. 34. Dance, N., Huehns, E. R., and Shooter, E. M. (1964) Biochim. Biophys. Acta 86, 144.

Traverse, P. M., Lehmann. H.. Coquelet, M. L., Beale, D., and Isaacs. W. A. (1966) C. R. Sot. Biol. 160, 2270. 36. Wade, P. T., Jenkins. T., and Huehns, E. R. (1967) Natwe (London) 216, 688. 37. Bratu. V., Lorkin, P. A., Lehmann, H., and Predescu, C. (1971) B~of~~irn. Biophys. Actn 251, I. 38. Brimhall, B.. Hollan, S.. Jones, R. T., Koler, R. D., Stocklen, Z., and Szelenyi. J. G. (1970) Clin. Res. 18, 184. (See also ref. 15 1) 38a. O’Brien, C., Gray. M. J., and Jacob, A. S. (1964) Amer. J. Obstet. Gynecol. 88, 816. 39. Hunt, J. A., and Ingram, V. M. (1959) Nature (London) 184, 640. 40. Sick, K.. Beale, D., Irvine. D., Lehmann, H.. Goodall, P. T., and MacDougall, S. ( 1967) Biochim. Biophys. Actn 140, 23 I. 41. Wade, P., Yates, A., Bellingham, A. J., and Huehns, E. R.. cited by Huehns, E. R. (1970) Bull. Sot. Chim. Biol. 52, 1145. 42. Allan, N., Beale. D., Irvine, D.. and Lehmann, H. (1965) Natwe (London) 208, 658. 43. Botha, M., Beale, D., Isaac?,, W. A., and Lehmann. H. (1966) Natwe (London) 212, 792. 44. Jones, R. T., Koler, R. D., Duerst. M., and Stocklen. Z. (1972) Advan. Exp. Med. Biol. 28, 79. 45. Boyer, S. H., Crosby, E. F.. Fuller, C. F.. Ulenurm, L., and Buck, A. A. ( 1968) Amer. J. Hum. Genet. 20, 570. 46. Jones. R. T.. Brimhall, B., and Lisker. R. (1968) ~~~~~fi~n. ~~0~~~s. Ada 154, 488. 47. Baglioni, C. (1962) Biochim. Biophys. Acta 59, 437. 48. Josephson, A. M., Weinstein. H. G., Yakulis, V. J.. Singer, L.. and Heller, P. (1962) 3. L,ab. Clin. Med. 59, 918. 49. Blackwell, R. Q., Weng, M.-l.. Liu, C.-S., Shih, T.-B., and Wang. C.-L. (1972) VOX Sang 23,363. 50. Carrell, R. W.. and Owen. M. C. (1971) Biochim. Biophys. Acta 236, 507. 51. Bowman, B. H., Barnett, D. R.. and Hite, R. (1967) Biochem. Biophys. Res. Common. 26, 466. 5 la. Garel, M. C.. Cohen-Solal, M.. Blouquit. Y., and Rosa, J. (1974) Fed. Eur. Biothem. Sot. Lett. 43, 93. 52. Ross. J.. Oudart, J. L., Pagnier, J.. Belkhodja, O., Boigne, J. M.. and Labie, D. (I 968) Proc. Congr. Int. Sot. Hematol., 12th New York, p. 73. 52a. Labossiere. A.. Vella, F., Hiebert, J.. and Galbraith, P. ( 1972) C&n. Biochem. 5, 46. 53. Wiltshire, B. G., Clark, K. G. A., Lorkin, P. A., and Lehmann, H. (1972) B&x&m. Biophys. Actor 278, 459. 35.

AMINO

ACID

ANALYSES

OF PROTEINS.

IX

493

54. Marengo-Rowe, A. J., Lorkin, P. A., Gallo, E., and Lehmann. H. (1968) Biochim. Biophys. Acta 168, 58. 55. Schneider, R. G., Gustavson, L. P., Haggard, M. E., Brimhall, B.. and Jones, R. T. (1970) Proc. Intr. Congr. Hematol. 13th, Munich, cited in World Health Organ. Tech. Rep. Ser. No. 509, p. 58. 56. Beutler, E., Lang. A.. and Lehmann, L. (1974) Blood 43, 527. 57. Hunt, J. A., and Ingram, V. M. (1961) ~~~~c~zj~~,~i~phy~. Acta 49, 520. 58. Labossiere. A.. Hili, J. R., and Vella, F. (1971) f/in. B&hem. 4, 114. 59. Crookston, J. N., Farquharson, H. A., Beale, D.. and Lehmann. H. (1969) Can. J. Biochem. 47, 143. 60. Baglioni, C., cited by Huehns, E. R.. and Shooter, E. M. (1965) .I. Med. Getter. 2, 48. 61. Jones, R. T., Brimhall. B.. and Huisman, T. H. J. ( 1966) C/in. Res. 14, 168. 62. Schneider, R. G., Brimhall, B., Jones, R. T.. Bryant. R., Mitchell, C. B., and Goldberg, A. I. (1971) Biochim. Biophys. Acta 243, 164. 63. Jones, R. T., Brimhall, B., H&man, T. H. J.. Kleihauer. E., and Betke, K. (1966) Science 154, 1024. 64. Bowman, B. H., Oliver, C, P.. Barnett, D. R., Cunningham. J. E.. and Schneider, R. G. (1964) Blood 23, 193. 65. Sansone. G.. Carrell, R. W.. and Lehmann, H. (1967) Nature (London) 214, 877. 66. Huisman, T. H. J., Adams, H. R.. Wilson, J, B.. Efremov, G. D., Reynolds, C. A., and Wrightstone, R. N. (1970) Biochim. Biophys. Acta 200, 578. 66a. Hansen. H. A., Jagenburg, 0. R., and Johansson, B. G. (1960) Actu Puediut. 49, 503. 67. Bradley, T. B., Wohl, R. C., and Rieder. R. F. (1967) Science 157, 1581. 68. Colombo, B., Vidal. H., Kamuzura, H., and Lehmann, H. (1974) ~j~~c~zjm, Bio~~z~~. Rctu

351,

1.

69. Gehring-Mulier, R., Braunitzer, G., Kieihauer. E., and Betke, K. (1966) Hoppe Seyler’s Z. Physiol. Chem. 345, 18 1. 70. Dacie, J. V., Shinton, N. K., Gaffney, P. J., Carrell. R. W., and Lehmann. H. (1967) Nature (London) 216, 663. 71. Bookchin, R. M., Nagel. R. L., Ranney, H. M., and Jacob, A. S. (1966) Bio&em. Biophys. Res. Common. 23, 122. 72. Halbrecht, I., Isaac& W. A., Lehmann, H., and Ben-Porat, F. (1967) Israel J. Med. Sei. 3, 827. 73. (a) White, J. M.. Szur, L., Gilles, 1. D. S.. Lorkin, P. A.. and Lehmann. H. (1973) Brit. Med. .I. 3, 665. (b) White, J. M.. Szur. L., Roberts, P., Lorkin, P. A.. and Lehmann, H. (1973) Brit. J. Haematol. 25, 284. 74. Boulton. F. E., Huntsman, R. G.. Lehmann, H., Lorkin. P., and Herrera, A. E. R. (1970) Biochem. J. 119, 69P. 75. Miyaii, T., Oba, Y., Yamamoto, K., Shibata, S., Iuchi. I., and Hamilton, H. B. (1968) Science 159, 204. 74. Shibata, S.. Miyaji, T., luchi, I., Ueda, S.. and Takeda, I. ( 1964) C&n. Chink. Acta 10, 101. 77. Yanase, T., Hanada, M., Seita, M.. Ohya, I., Ohta, Y.. Imamura, T., Fujimura, T., Kawasaki, K., and Yamaoka, K. (1968) Jap. 1. Hum. Genet. 13, 40. 78. Perutz, M. F., Pulsinelli, P., TenEyck, L., Kilmartin. J. V., Shibata, S., Juchi, I., Miyaji. T., and Hamilton, H. B. (1971) Nature Neu* Biol. 232, 147. 79. Miyaji, T., Ohba, Y., Yamamoto, K.. Shibata, S., luchi, 1.. and Takenaka, M. (1968) Nature (London) 217, 89. 80. (a) Blackwell. R. Q., and Liu, C.-S. (1970) Biochirn. Bi&p. hta 200, 70.

494

81. 82. 83. 84. 85. 86. 87. 88. 89. 90. 91. 92. 93. 94. 95. 96. 97. 98. 99.

100.

DONALD

M.

KIRSCHENBAUM

(b) Blackwell, R. Q.. Liu, C.-S., and Wang, C. L. (1972) VOX Sang 23, 433. Swenson, R. T., Hill, R. L.. Lehmann. H., and Jim, R. T. S. (1962) J. Bio/. Chem. 237, 1517. Minnich, V., Hill, R. J., Khuri, P. D., and Anderson, M. E. (1965) Blood 25, 830. Gottlieb. A. J., Robinson, E. A.. and Itano, H. A. (1967) Nnfure (London) 214, 189. Charache. S., and Ostertag, W. (1970) Blood 36, 852. Blackwell, R. Q., Shih, T.-B., Wang, C. L.. and Liu. C.-S. (1972) Biochim. Biophys. Acta 257, 49. Blackwell. R. Q.. Liu. C.-S.. Yang, H.-J., Wang. C.-C., and Huang, J. ( 1968) Science 161, 381. Sacker. L. S., Beale, D., Black, A. J.. Huntsman, R. G., Lehmann. H., and Lorkin, P. A. (1967) Brit. Med. J. 3, 53 1. Heller. P., Coleman, R. D., and Yakulis, V. (1966) J. C/in. Initest. 4.5, 102 I. Beale, D., and Lehmann, H. (1965) Nature (London) 207, 259. Watson-Williams, E. J., Beale, D., Irvine, D., and Lehmann. H. (1965) Nature (London) 205, 1273. Sukumaran. P. K., Wiltshire, B. G.. and Lehmann, H. (1971) Proc. 2nd Meeting Asian-Pacjfic Di,Gion, Int. Sot. Hematol. Melbourne, p 14. Eng, L. I. L.. Pribadi, W., Westendorp-Boerma. F., Efremov. G. D.. Wilson, J. B.. Reynolds, C. A., and Huisman. T. H. J. (I 971) Biochim. Biophys. Acta 229, 335. Sansone, G.. Centa, A., Sciarratta, V., GaIIo, E.. and Lehmann, H. (1970) Acta Haematol. 43, 40. Marti, H. R., Pik. C.. and Mosimann, P. (I 964) Acta Haematol. 32, 9. (a) Rahbar, S. (1973) .I. Haematol. 24, 31. (b) Rohe, R. A.. Sharma, V., and Ranney, H. M. (1973) Blood 42, 455. Rahbar, S., Beale, D.. Isaacs, W. A., and Lehmann, H. ( 1967) Brit. Med. J. 1, 674. Lorkin, P. A., Charlesworth, D., Lehmann, H., Rahbar. S.. Tuchinda, S., and Eng, L. I. L. (I 970) Brit. J. Haematol. 19, 117. Dance, N., Huehns. E. R.. and Shooter, E. M. cited in Schroeder. W. A., and Jones, R. T. (1965) Progr. Chem. Org. Natur. Prod. 23, 113. Aksoy, M., Erdem. S.. Efremov, G. D., Wilson. J. B.. Husiman. T. H. J., Schroeder, W. A., Shelton. J. R., Shelton, J. B., Ulitin, 0. N., and Muftuoglu, A. (1972) J. C/in. Invest. 51, 3380.

Miyaji, T., Iuchi, I., Shibata, S., Takeda, I., and Tamura, A. (1963) Acta Haematol. Jap. 26, 538. 101. Ahern, E. J., Jones, R. T., Brimhall. B., and Gray, R. H. (1970) Brit. J. Haematol. 18, 369. 102. Dobbs. N. B., Simmons, J. W., Wilson, J. B.. and Huisman, T. H. J. (1966) Biochim. Biophys. Acta 117, 492. 102a. Jones, R. T.. Coleman, R. D., and Heller, P. ( 1966) J. Biol. Chem. 241, 2 137. 103. Bonaventura, J., and Riggs, A. (1968). J. Biol. Chem. 243, 80. 104. Blackwell, R. Q., Liu. C.-S.. and Shih, T.-B. (1971) Biochim. Biophys. Acta 229, 343. 105. Reed, C. S., Hampson. R.. Gordon, S., Jones, R. T.. Novy, M. J., Brimhall. B., Edwards, M. J., and Koler. R. D. (1968) Blood 31, 623. 106. Helter. P. cited by Hamilton, H. B., Iuchi, I., Miyaji, T., and Shibata. S. (1969) J. Clin. Invest. 8, 525. 107. Clegg, J. B., Weatherall. D. J., Boon, W. H., and Mustafa, D. (1969) Nature (London) 222, 379. 108. Hollan, S. R., Szelenyi, J. G., Lehmann. H., and Beale, D. (1967) Hematologia 1, 11. 109. Chernoff, A. I. (1965) Biochim. Biophys. Acta 97, 47.

AMINO

ACID

ANALYSES

OF

PROTEINS.

495

IX

110. Marti, H. R., Beale, D., and Lehmann, H. (1967) Acta Haematol. 37, 174. 111. Hanada. M., Rucknagel, D. L.. and Cohen, M. M. cited in Schroeder. W. A., and Jones, R. T. (1965) Progr. Chem. Org. Natur. Prod. 23, 113. 112. Carrell, R. W., Lehmann. H.. and Hutchison. H. E. (1966) Nature (London) 210, 915. 113. Blackwell, R. Q., and Liu, C.-S. (1966) Biochem. Biophys. Res. Commun. 24, 731. 114. Konotey-Ahulu. F. I. D.. Gallo, E., Lehmann, H., and Ringelhann. B. J. (1968). J. Med.

Genet.

5, 107.

115. Shibata, S., Miyaji. T., Iuchi. I., Ueda, S., Takeda, I.. Kimura, N., and Kodamd, S. (1962) Acta Haematol. Jup. 25, 690. 116. De Jong, W. W., Went. L. N., and Bernini. L. F. (1968) Nature (London) 220, 788. 117. Bare, G. N.. Alben. J. O., Bromberg, P. A., Jones, R. T., Brimhall. B.. and Padilla, F. (1974) .I. Biol. C/Tern. 249, 773. 117a. Cohen-Solal, M., Blouquit. Y.. Care]. G.. Thillet, J., Lazare. G.. Creyssel, R.. Gibaud. A.. and Rosa, J. (1974) Biochim. Biophys. Acta 351, 306. 118. Pootrakul, S.. and Dixon, G. H. (1970) Can. J. Biochem. 48, 1066. 119. Blackwell, R. Q.. Oemijati. S., Pribadi, W., Weng, M.-l.. and Liu. C.-S. (1970) Biochim.

Biophys.

Acta

214,

396.

120. Eng. L. I. L., Kamuzord, H., and Lehmann, H. (1974) J. Med. Genet. 11, 25. 121. Lorkin. P. A., Lehmann. H.. Fairbanks, V. F., Berglund. G., and Leonhardt, T. (1970) Biochem. J. 119, 68P. 127. Cauchi, M. N.. Clegg. J. B.. and Weatherall, D. J. (1969) Natare (London) 223, 3 1 I, 123. Blackwell. R. Q.. Liu. C.-S.. Lie-lnjo. L. E., and Pribadi. W. (1970) ~,,lc,.. J. p/1~,~. Anthropol. 32, 147. 124. Crookston. J. H., Farquharson, H. A., Kinderlerer, J. L., and Lehmann, H. (1970) Can. J. Biochem. 48, 9 1 1. 125. Gottlieb, A. J., Restropo. A., and Itano. H. A. (1964) Fed. Proc. 23, 172. 126. Blackwell. R. Q.. Wong. H. B.. Wang, C. L.. Weng. M. 1.. and Liu, C. S. (1974) Biochim.

Biophys.

Acta

351.

7.

126a. Sharma, R. S.. Harding, D. L.. Wong, S. C., Wilson, J. B., Gravely, M. E.. and Huisman. T. H. J. (1974) Eiochim. Biophys. Acta 359, 233. 127. Kraus, L. M., Miyaji, T.. luchi, I., and Kraus, A. P. (1966) Biochemistry 5, 3701. 118. Kraus, L. M. cited in Schroeder, W. A., and Jones, R. T. (1965) Progr. Chem. Org. Nat. Prod. 23, 1 13. 129. Jones, R. T., Koler. R. D.. and Lisker. R. (1963) Cli,l. Res. 11. 105. 130. Idelson. L. I., Didkowsky, N. A., Casey, R., Lorkin, P. A., and Lehmann. H. (1974) Nutare

(Lorzdon)

249, 768.

13 1. Maekawa. M., Maekawa. T.. Fujiwara. N.. Tabara, K.. and Matsuda, G. (1970) Int. J. Prot. Res. 2, 147. 132. Chernoff. A. I., and Perillie. P. E. (1964) Biochem. Biophys. Res. Commun. 16, 368. 133. Ranney. H. M.. Jacobs. A. S., and Nagel, R. L. (1967) Nature (London) 213, 876. 134. Baglioni, C. (1962) J. Biol. Chem. 237, 69. 135. Huntsman, R. G., Lorkin. P. A., and Lehmann. H. (1972) cited in Aflus Protein Sequence

Strut.

5, 85.

135a. Gordon-Smith, E. C.. Dacie, J. V., Blecher. T. E.. French, E. A,, Wiltshire, B. G.. and Lehmann. H. (1973) Proc. Roy. Sot. Med. 66, 507. 136. Kendall, A. G.. Barr, R. D., Lang. A., and Lehmann, H. (1973) Biochim. Biophys. Acta

310,

357.

136a. Ranney, H. M.. Jacobs, A. S., Ramot, B.. and Bradley, T. B., (1969)5. C/in. Invest. 48, 2057.

137. Kraus. L. (1972) cited in World

Health

Organ.

Tech.

Rep.

No.

509,

p, 55.

496

DONALD

M.

KIRSCHENBAUM

137a. Imamura, T., and Riggs, A. (1972) Biochem. Genet. 7, 127. 138. Beresford, C. H., Clegg, J. B., and Weatherall, D. J. (1972) J. Med. Genet. 9, 151. 139. Pik, C., and Tonz, 0. (1966) Nature (London) 210, 1182. 140. Stamatoyannopoulos, G., Nute. P. E., Adamson. J. W.. Bellingham. A. J., and Funk, D. (1973) J. Clin. Invest. 52, 342. 141. Elion, J., Belkhodja. O., Wajcman, H., and Labie, D. (1973) Biochim. Biophys. Actu 310,

360.

142. Shimizu, A., Hayashi. A.. Yamamura, Biochim.

Biophys.

143. Konotey-Ahulu, J. Med.

Genet.

Acta

Y., Tsugita, A., and Kitayama,

K. (1965)

97. 472.

F. I. D., Kinderlerer,

J. L., Lehmann, H.. and Ringelhann, B. (1971)

8, 302.

144. Liddell. J., Brown, D.. Beale, D., Lehmann, H.. and Huntsman, R. G. (1964) Nature (London)

204, 269.

145. Schneider, R. G., Alperin, J. B., Brimhall, B., and Jones, R. T. (1969) J. Lab. Med.

C/in.

73, 616.

146. Labie, D., and Schapira, G. (1966) Nature (London) 209, 1033. 147. Rosa, J.. Maleknia, N., Vergoz, D., and Dunet, R. (1966) Nouv. Rev, Fr. Hematol. 6, 423.

148. Labie, D., and Rosa, J. (1966) Now. Rev. Fr. Hematol. 6, 426. 149. Rahbar, S., Kinderlerer, J. L., and Lehmann, H. (1969) Acta Haematol. 42, 169. 150. Yates. A., Jackson, J. M., and Huehns, E. R. (1972) cited in World Health Organ. Tech. Rep. No. 509, p. 57. 1.51. Brimhall, B.. Duerst, M., Hollan, S. R., Stenzel, P., Szelenyi, J., and Jones, R. T. (1974) Biochim. Biophys. Acta 336, 344. (See also ref. 38) 152. King, M., Wiltshire. B. G., Lehmann, H., and Morimoto, H. (1972) Brit. J. Haematol.

22, 125.

153. Baglioni, C., and Ingram, V. M. (1961) Biochim. Biophys. Acta 48, 253. 154. Rieder. R. F., Oski, F. A., and Clegg, J. B. (1969) J. C/in. Invest. 48, 1627. 155. Bowman, B. H., Oliver, C. P. Barnett, D. R.. Cunningham, J. E.. and Schneider, R. G. (1964) Blood 23, 193. 156. Bonaventura, J.. and Riggs, A. (1967) Science 158, 800. 156a. Tondo, C. V. (1972) An. Acud. Brasil. Cienc. 44, 377. 157. Murawski, K., Carta, S., Sorcini, M., Tentori. L., Vivaldi, G.. Antonini, E., Brunori, M.. Wyman, J., Bucci. E., and Rossi-Fanelli, A. ( 1965) Arch. Biochem. Biophys. 111,

197.

158. Hyde, R. D., Kinderlerer. J. L., Lehmann, H., and Hall, M. D. (1971) Biochim. Biophys. Acta 243, 5 15. 159. Salomon, H., Tatarski, 1.. Dance, N., Huehns, E. R., and Shooter, E. M. (1965) Israel

J. Med.

Sci.

1, 836.

160. De Jong, W. W., Bernini, L. F.. and Khan, P. M. (1971) Biochim. Biophys. Acta 236, 197. 161. Efremov, G. D., Huisman, T. H. J., Smith. L. L.. Wilson, J. B., Kitchens, J. L., Wrightstone, R. N., and Adams, H. R. (1969) J. Biol. Chem. 244, 6105. 162. Ranney. H. M., Jacobs, A. S.. Udem, L., and Zalusky, R. (1968) Biochem. Biophys. Res. Commun. 33, 1004. 163. Alberti, R., Mariuzzi, G. M., Artibani, L.. Bruni, E., and Tentori. L. (1974) Biochim. Biophys.

164. 165. 166. 167.

Acta

342,

1.

Adams, J. G., Winter, W. P., Tausk, K., and Heller, P. (1974) Blood 43, 261. Reynolds, C. A., and Huisman, T. H. J. (1966) Biochim. Biophys. Acta 130, 541. Ingram, V. M. (1957) Nature (London) 180, 326. Schneider. R. G., Ueda, S., Alperin, J. B., Brimhall, B., and Jones, R. T. (1969) N. Engl.

J. Med.

280, 739.

AMINO

ACID

ANALYSES

OF PROTEINS.

IX

497

168. Wajcman, H., Labie. D., and Schapira, G. (1973) Biochim. Biophys. Acta 29.5, 495. 169. Beuzard, Y., Courvalin, J. C., Cohen-Solal, M., Garel. J., Rosa. J.. Brigard, C. P., and Gibaud, A. ( 1972) Fed. Eur. Biochem. Sot. Lett. 27, 76. 170. Cohen-Solal, M.. Seligmann. M., Thillet. J., and Rosa, J. (1972) Proc. In!. Congr. Hematol. 14th Sao Paulo. abstr. 408. 171. Bannister, W. H., Grech, J. L., Plese, C. F.. Smith, L. L.. Barton, B. P.. Wilson, J. B., Reynolds. C. A., and Huisman, T. H. J. (1971) Eur. J. Biochem. 29, 301. 171a. Nute, P. E.. Stamatoyannopoulos, G., Hermodson. M. A., and Roth, D. ( 1974) J. Clin.

Invest.

53, 320.

171b. Hill, R. I., Swenson, R. T.. and Schwartz, H. C. (1960) /. Biol. Chem. 235, 3182. 172. Opfell, R. W., Lorkin, P. A., and Lehmann, H. (1968) J. Med. Getlet. 5, 291. 173. Tangheroni. W., Zorcolo. G.. Gallo. E.. and Lehmann, H. (1968) Nature (London) 218, 470. 173a. Vella. F., Lorkin, P. A.. Carrell. R. W.. and Lehmann, H. (1967) Can. J. Biochem. 45, 1385. 174. Vella, F., lsaacs, W. A., and Lehmann, H. (1967) Can. J. Biochem. 45, 3.5 1. 174a. Labossiere. A.. and Vella, F. (1971) C/in. Biochim. 4, 104. 175. Huisman, T. H. J.. Brown, A. K.. Efremov, G. D., Wilson, J. B., Reynolds, C. A., Uy, R., and Smith, L. L. (1971)3. C/in. Invest. 50, 650. 176. Sumida, I.. Ohta. Y., Imamura. T., and Yanase, T. (1973) Biochim. Biophys. Acta 322, 23. 177. Schneider, R. G.. Ueda. S., Alperin. J. B., Brimhall. B., and Jones, R. T. (1968) Amer. .I. Hum. Genet. 20, 151. 178. Huehns. E. R., Hecht, F., Yoshida. A., Stamatoyannopoulos. G.. Hartman. J.. and Motulsky, A. G. (1970) Blood 36, 209. 179. Jones, R. T., Brimhall. B., Huehns, E. R., and Motulsky. A. G. (1968) Biochim. Biophys. Acta 154, 278. 180. White, J. M., Brain, M. C., Lorkin, P. A., Lehmann. H.. and Smith, M. ( 1970) Natwe

(London)

225, 939.

181. Miyaji, T., Iuchi. I., Takeda, 1.. and Shibata, S. (1963) Acra Haemorol. Jap. 26, 531. 182. Ricco, G., Pith, P. G., Mazza, U.. Rossi. G., Ajmar, F.. Arese, P.. and Gallo, E. (1974) Fed. Eur. Biochem. Sot. Lett. 39, 200, 182a. Pootrakul, S., Srichiyanont, S., Wasi. P., and Suanpon, S. (1974) Humongenerik 23, 199. 183. Ostertag, W., and Smith, E. W. (1968) Humangenetik 6, 377. 184. Blackwell. R. Q., Boon, W. H., Liu, C. S., and Weng, M. I. (1972) Biochim. Biophys. Acta

185. 186. 187. 188. 189. 190. 191. 192. 193. 194.

278, 482.

Tuchinda. S., Beale. D., and Lehmann, H. (1965) Brit. Med. J. 1, 1583. Baur, E. W. (1968) Humangenetik 6, 368. Monn, E., Gaffney, P. J., and Lehmann, H. (1968) Stand. J. Haematol. 5, 353. Hyde, R. D., Hall, M. D., Wiltshire, B. G., and Lehmann, H. (1972) Lancet 2, 1170. Jones, R. T.. Brimhall, B., Huehns, E. R., and Barnicott, N. A. (1966) Science 151, 1406. Schneider, R. G., and Bowman, B. H. cited by Schroeder, W. A., and Jones, R. T. (1965) Progr. Chem. Org. Nat. Prod. 23, 113. van Ros, G., Beale, D., and Lehmann, H. (1968) Brit. Med. J. 4, 92. Bowman, B. H., Barnett, D. R.. Hodgkinson, K. T., and Schneider, R. G. (1966) Nature (London) 211, 1305. Carrell, R. W.. Lehmann. H., Lorkin. P. A.. Raik, E., and Hunter, E. (1967) Nature (London) 215, 626. Blackwell, R. Q.. Yang, H. J.. and Wang, C. C. (1969) Biochim. Biophys. Acta 188, 59.

498 195. 196. 197. 198. 199. 200. 201. 202. 203. 204. 205. 206. 207. 208. 209. 210. 211. 212. 213. 214. 21.5. 216. 217. 218. 219. 220. 221.

222. 223. 224.

DONALD

M.

KIRSCHENBAUM

Baur, E. W.. and Motulsky. A. G. (1965) Humungenefik 1, 62 1. Blackwell. R. Q., Huang, J. T. H.. and Ro, I. H. (1967) Science 158, 1056. Blackwell. R. Q.. Yang, H. J.. and Wang. C. C. ( 1969) Biochim. Biophys. Acttr 194, 1. Blackwell, R. Q.. and Liu, C. S. (1968) Biochem. Biophys. Res. Common. 30, 690. Blackwell. R. Q., Yang, H. J.. and Wang, C. C. (1969) Biochim. Biophys. Acta 175, 237. Elatz, G.. Kinderlerer. J. L., Kilmartin, J. V.. and Lehmann. H. (197 1) Luncet 1, 732. Blackwell, R. Q.. Lui. C. S.. and Wang. C. L. (1971) Biochim. Biophys. Acra 243, 467. Jenkins, G. C., Beale, D., Black, A. J., Huntsman, G. R., and Lehmann, H. (1967) Brit. J. Haematol. 13, 252. Larkin, 1. L. M., Baker, T., Lorkin. P. A., Lehmann, H., Black, A. J., and Huntsman. R. G. ( 1968) Brit. J. Haematol. 14, 233. Bowman, E. H., and Barnett, D. R. (1967) Nature (London) 214, 499. Wasi, P., Pootrakul, S., Na-Nakorn, S.. Beale, D.. and Lehmann, H. (1968) Acta Haematol. 39, 15 1. Shibata, S.. Miyaji, T., Ueda, S., Matsuoka, M., luchi, I., Yamada, K.. and Shinkai, N. (1970) Proc. Jap. Acad. 46, 440. Miyaji, T.. Takeda. I., and Shibata, S. (1963) Actn Haematol. Jap. 26, No. I (Suppl.). 45. Gajdusek. D. C.. Guiart. J., Kirk, R. L., Carrell, R. W., Irvine. D., Kynoch. P. A. M., and Lehmann, H. (1967) J. Med. Genet. 4. 1. Crookston. J. H., Beale. D.. Irvine, D., and Lehmann. H. (1965) Nature (London) 208, 1059. Berretta, A., Prato, V.. Gallo, E., and Lehmann, H. (1968) Nature (London) 217, 1016. Rosa. J.. Labie. D., Wajcman. H.. Boigne, J. M., Cabannes, R., Bierme, R., and Ruffie. J. (1969) Nature (London) 223, 190. Miyaji, T.. Iuchi, I.. Yamamoto, K., Ohba, Y.. and Shibata, S. (1967) Clin. Chim. Acta 16, 347. Fessas, P.. Kaltsoya. A., Loukopoulos, D., and Nilsson, L. 0. (1969) Hum. Hered. 19, 152. Blackwell, R. Q., Jim, R. T. S., Tan. T. G. H.. Weng, M. I., Liu. C. S., and Wang, C. L. ( 1973) Biochim. Biophys. Acta 322, 27. Gerald, P. S. cited by Weatherall, D. J.. Sigler, A. T., and Baglioni. C. (1962) Bull. Johns Hopkins Hosp. 111, 143. Pietschmann, H., Lorkin, P. A., Lehmann. H.. and Braunsteiner. H. (1972) cited in World Health Organ. Tech. Rep. No. 509, p. 56. Vella. F.. Wiltshire. B., Lehmann. H., and Galbraith, P. (1973) Clin. Biochem. 6. 66. Baglioni, C., and Ingram, V. M. (1961) Nature (London) 189, 465. Jones. R. T., Osgood, E. E., Brimhall, B.. and Koler, R. D. (1967)5. Clin. Im.est. 46, 1840. Imamura. T., Fujita. S.. Ohta, Y., Hanada, M.. and Yanase, T. (1969) J. C/in. Invest. 48, 2341. (a) Rucknagel, D. L., Glynn, K. P., and Smith, J. R. (1967) C/in. Res. 15, 270 (b) Rucknagel, D. L. cited in (197 1) Stamatoyannopoulos, G., Bellingham, A. J., Lenfant. C., and Finch, C. A. ( 197 1) Annu. Ret,. Med. 22, 22 I. Barclay, G. P. T., Charlesworth. D., and Lehmann, H. (1969) Brit. Med. J. 4, 595. Muller, C. J., and Kingma, S. (1961) Biochim. Biophys. Acta 50, 595. Labie, D.. Schroeder. W. A., Huisman, T. H. J. (1966) B&him. Biophys. Actu 127, 428.

AMINO

ACID

ANALYSES

OF PROTEINS.

IX

499

315. Ostertag, W., and Smith. E. W. (1969) Eur. J. Eiochem. 10, 37 I. 226. Baglioni, C., and Ventruto, V. (1968) Eur. 1. Bid&em. 5, 29. 726a. Labie, D., Pagnier, J., Mallarme, J., and Boivin. P. (1972) Ann. Biol. C/in. (Pnris) 29, 343.

126b. Rahbar, S.. Golban-Maghadam. N., and Saoodi. H. ( 1974) Blood 43. 79. 227. Curtain, C. C. ( 1964) AUG. J. Esp. Bid. 42, 89. 218. Ohta, Y.. Yamaoka, I(.. Sumida, I., and Yanase, T. (1971) Natwe Nero Bid. 218. 229. Badr, F. M., Lorkin. P. A., and Lehmann. H. (1973) Nutwe Nrrc Biol. 242, 230. (a) Clegg. J. B., Weatherall, D. J.. and Gilles, H. M. (1973) Nnfwr Nrrc Bid. 184. (b) Huisman. T. H. J.. Wrightstone. R. N.. and Wilson, J. B. (1972) Arch. them. Biophy. 153, 850.

234.

107. 246,

Bio-