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COAGULATED PROTEINS. 107
In the tabulation of the hydrolytic products of plant proteins we
give edestin, of the hemp-seed, and legumin of the pea as examples of
globulins. The other three, hordein of barley, gliadin of wheat and zein
from corn belong to the prolamine group.
Edestin.! Legumin.‘ Hordein.® Gliadin.? Zein.
Giyeocoll.... 2 200.65 3.8 0.38 0.0 0.689 0.0
ATRIA 6, (nical nt sheik 3.6 2.08 0.43 2.0 9:79
SIMO 5.6, a aceon" 5.6? 1.05 0.13 3.34 1.88
PAGUCIDG tire ektere shots 20.9 8.0 5.67 6.62 19.55
oa a oe ee 0.33 0.53 —_— 0.13 1.02
Aspartic acid...... 4.5 5.3 —_ 0.58 Lah
Glutamic acid...... 18.748 13.8 43.197 43 .66 26.17
OS ee 0.25 — — 0.45 _—
Phenylalanine...... 2.4 3.75 5.03 2.35 6.55
mytosine s/s. S a1 1.55 LGT 1.20 3.55-10.i"4
EB ai pe een’s Lh 3.22 13.73 13.22 9.04
Oxuproline... ..:,..: 2.0 — — — =
Tryptophane....... 0.38}? —_ — 1.00 _—
PGI oo 5 oie hss rae 2.42 1.28 0.61 0.82
A i bay A 10.12 2.16 Sle ees
yeme. 23S... 1.0 4.29 0.00 0.00 0.00
(ATOM OMNIS s fis ys: <5 _ 1.49 4.87 5.22 3.61
Coagulated Proteins. Proteins may be converted into the coagu-
lated condition by different means: by heating, by the action of alcohol,
especially in the presence of neutral salts, by chloroform, ether, and
metallic salts, and by the prolonged shaking of their solutions and in
certain cases, as in the conversion of fibrinogen into fibrin (Chapter V),
by the action of an enzyme. The nature of the processes which take
place during coagulation is unknown. The coagulated albuminous
bodies are insoluble in water, in neutral salt solutions, and dilute acids
or alkalies, at normal temperature. They are dissolved and converted
into albuminates by the action of dilute acids or alkalies, especially
on heating.
Coagulated proteins also seem to occur in animal tissues. We find,
at least in many organs such as the liver and other glands, proteins
1 Abderhalden, Zeitschr. f. physiol. Chem., 37 and 40.
2 Levene and D. v. Slyke, Journ. of biol. Chem., 6.
3 Osborne and Biddle Amer. Journ. of Physiol, 26.
4 Osborne and Clapp, Journ. of biol. Chem. 3.
5 Abderhalden and Babkin, ibid., 47.
6 Osborne and Clapp, Amer. Journ. of Physiol., 19.
7 Osborne and Jones, ibid., 26.
8 Osborne and Guest, Journ. of biol. Chem., 9.
® Abderhalden and Samuely, Zeitschr. f. physiol. Chem., 44.
10 Osborne, Jones and Clapp, Amer. Journ. of Physiol., 26.
41 Kutscher, Zeitschr. f. physiol. Chem., 38.
12 Fasal, Bioch. Zeitschr., 44.
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