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General. Continued
In view of the marked differences in structure existing among these amino acids it
becomes important to know the relative proportions in which the various amino acid
radicles exist in the different proteins. This is studied by hydrolyzing the protein and
separating and recovering as completely as possible the amino acids resulting from
the hydrolysis. Since the recovery of the amino acids cannot be accomplished without
loss, the results obtained are not strictly quantitative and our knowledge of the
radicles which make up the protein molecule remains incomplete. It is believed by the
investigators who have given most attention to the question that the failure of the
recovered amino acids to show a summation of one hundred per cent is more probably
due to unavoidable losses in estimating the known amino acids than to the presence of
other amino acids not yet identified. The accompanying table shows the percentages
of amino acids obtained from four proteins occurring in different food materials.
Percentages Of Amino Acids From Four Different Proteins
Casein
Gelatin
(from
Milk)
Gliadin
Zein
(from
(from
Maize)
Wheat)
Glycin...............................
o.oo
16.5
0.00
0.00
Alanine.............................
1.50
0.6
2.00
13.39
Valine...............................
7.20
1.
334
1.88
Lecine...............................
9.35
9-2
6.62
19.55
Proline.............................
6.70
10.4
13.22
9.04
1.39
1.2
0.58
1.71
Glutamic acid.................................
15.55
16.8
43.66
26.17
Phenylalanine..................................
3.20
1.
2.35
6.55
Tyrosine..........................
4.50
0.
1.50
3.55
Serine...............................
.50
.4
.13
1.02
Oxyproline..........................
.23
3.0
Histidine..........................
2.50
1.84
.82
Arginine...........................
3.81
93
3.16
1.55
Lysine...............................
7.61
6.
0.92
0.00
Tryptophane ....................................
1.5
0.0
1.0
0.00
Cystine.............................
.06
.45
Ammonia.........................
1.61
.4
5.22
3.64
Summation.....
67.21
76.21
85.67
88.87
From the data given in the table it will be seen that the proportions in which a given
amino acid radicle occurs in various proteins may be quite different. The four proteins
here shown yield from o.o to 16.5 per cent of glycine; from 0.6 to 9.8 per cent of
alanine; from 1.0 to 7.2 per cent of valine, from 6.6 to 19.6 per cent of leucine. Of
lysine, zein yields none, gliadin about 1 per cent, gelatin 6 per cent, and casein about
8 per cent. Of tryptophane, zein and gelatin yield none, gliadin about 1 per cent,
casein about 1.5 per cent.
* In general each figure given in the table is the highest of the results reported in
recent investigations. This is deemed more accurate than to give average results,
because of the unavoidable losses referred to above.
The data given for casein, gliadin, and zein are taken chiefly from the work of
Osborne and his associates; those for gelatin chiefly from that of Skraup and Behler.
For more detailed comparisons of the percentages of amino acids in different proteins
and also in the flesh of four widely separated species, the more extended table further
on in this chapter may be consulted. Whether it be essential that the proteins of the
food shall furnish all the amino acids which the body proteins contain will naturally
depend upon whether the body is able to make individual amino acids or not.
Experimental evidence has shown that the animal body can make glycine readily, so
that the absence of glycine radicles in the food proteins does not detract from their
nutritive value. On the other hand the animal body does not seem able to make
tryptophane, and as this is an essential constituent of body tissue the food protein
must always furnish tryptophane if it is to meet the needs of animal nutrition. Feeding
experiments have also shown that the rate of growth of young animals may be largely
influenced by the lysine content of the proteins fed; food proteins in which lysine is
lacking or inadequate may suffice for the maintenance of full grown animals but fail
to support normal growth in the young of the same species.
Such facts as these make it important that we study the proteins not only as a group
but also individually and that we learn as much as possible about the kinds and
amounts of amino acid radicles in the individual proteins.
The ultimate composition of the proteins shows a general similarity throughout the
group. All contain carbon, hydrogen, oxygen, nitrogen, and sulphur; some also
phosphorus or iron.
Composition Of Some Typical Proteins According To Osborne
Carbo
n per
Hydrog
en per
Nitroge
n per
Oxyge
n
Sulph
ur
Iron
per
Phosphor
us per
CEN
T
CENT
CENT
PER
CENT
PER
CENT
CEN
T
CENT
Egg-albumin
52.7s
7.10
15.51
23.02
4
I.6l6
Lactalbumin .
52.19
7.18
15.77
23.13
1.73
Leucosin . . .
53.02
6.84
16.80
22.06
1.28
Serumglobulin
52.71
7.01
15.85
23.32
1.11
Myosin . . .
52.82
7.11
16.67
22.03
1.27
Edestin . . .
51.50
7.02
18.69
21.91
O.88
Legumin . . .
51.72
6.95
18.04
22.00
5
0.385
Casein . . .
53.13
7.06
15.78
22.37
0.80
0.86
Ovovitellin . .
51.56
7.12
16.23
23.24
2
I.028
0.82
Gliadin . . .
52.72
6.86
17.66
21.73
3
I.027
Zein ....
55.23
7.26
16.13
20.78
0.60
Oxyhemoglob
in
54.64
7.09
17.38
20.I65
0.39
0.33
5
It will be seen that all these typical proteins contain 51 to 55 per cent carbon, about 7
per cent hydrogen, 20 to 23 per cent oxygen, 15.5 to 18.7 per cent nitrogen, 0.3 to 2.0
per cent sulphur. Other typical proteins thus far studied have shown ultimate
composition within these same limits.
Similarity of elementary composition is entirely consistent with the belief that there
may be an enormous number of chemical individuals among the proteins of nature.
Fischer has recently illustrated the vast number of isomers which may exist among
polypeptids and proteins by pointing out that a synthetic 19-peptid obtained by linking
15 glycine and 4 leucine molecules is only one of 3876 possible isomers, without
considering the tautomerism of the pep-tid linking. When more than two kinds of
amino acids are involved, the possible number of isomers increases very rapidly. If a
protein be imagined made up of 30 molecules of 18 different amino acids, one taken
twice, one 3 times, another 3, one 4, one 5 times, and 13 taken once each, there would
be 1027 isomers even if there were no tautomerism of the peptid group and if the
linking took place only in the simple way as with monamino-mono-carboxylic acids.
It is easy to see that when one considers not only isomerism but the vast number of
compounds of slightly different composition which can be obtained by varying the
kinds and proportions of the amino acid radicals in the protein molecule, the possible
number of different proteins of very similar elementary composition is practically
unlimited.
Probable Molecular Weights
From the results of ultimate analysis an approximate indication of the minimum
molecular weight may often be obtained by a very simple calculation. Thus,
oxyhemoglobin contains only 0.335 per cent of iron,and since there must be at least
one iron atom in the molecule, it is obvious from a simple proportion making use of
the atomic weight of iron, 0.335: 56:: 100 : x, that the molecular weight of