On Digestive Proteolysis: Being the Cartwright Lectures for 1894Chittenden, R. H. (Russell Henry)
Science
On Digestive Proteolysis: Being the Cartwright Lectures for 1894
Chittenden, R. H. (Russell Henry)
Digestion; Digestive enzymes; Enzymes
The fact that we have so many representatives of the hemi-group in
this decomposition is significant of the readiness with which the
so-called hemi-group undergoes change. All of its members are prone
to suffer hydration and cleavage, passing through successive stages
until leucin, tyrosin, and other simple bodies are reached. These,
and other similar crystalline bodies, are likewise the typical
end-products of proteolysis by trypsin, and presumably come directly
from the breaking-down of hemipeptone. Antipeptone, on the other
hand, is incapable of further change by the proteolytic ferment
trypsin. Hence, the hemi-group can be identified by the behavior of
the body containing it toward trypsin; _i.e._, it will ultimately
yield leucin, tyrosin, and other bodies of simple constitution to be
spoken of later on. The anti-group, however, will show its presence by
a certain degree of resistance to the action of trypsin, antipeptone
being the final product of its transformation by this agent; _i.e._,
leucin, tyrosin, etc., will not result. In this hydrolytic cleavage
of proteids the anti-group does not always appear as antialbumid. It
may make its appearance in the form of some related body, the exact
character of the product being dependent in great part upon the nature
of the hydrolytic agent, but in every case the characteristics of the
anti-group will come to the surface when the body is subjected to the
action of trypsin.
The above-described treatment of a coagulated proteid with water
containing sulphuric acid evidently induces profound changes in the
proteid molecule. The conditions are certainly such as favor hydration,
and in the case of complex molecules, like the proteids, cleavage might
naturally be expected to follow. Analysis of antialbumid from various
sources plainly shows that its formation is accompanied by marked
chemical changes. Thus, the following data, showing the composition of
antialbumid formed from egg-albumin and serum-albumin by the action
of dilute sulphuric acid at 100° C., gives tangible expression to the
extent of this change:
===========================================================
| |Antialbumid[87]| | Antialbumid[87]
| Egg- | from | Serum- | from
|albumin.| egg-albumin. |albumin.| serum-albumin.
--------+--------+---------------+--------+----------------
C.......| 52.33 | 53.79 | 53.05 | 54.51
H.......| 6.98 | 7.08 | 6.85 | 7.27
N.......| 15.84 | 14.55 | 16.04 | 14.31
--------+--------+---------------+--------+----------------
[87] Kühne und Chittenden: Zeitschr. f. Biol., Band 19, pp. 167 and 178.
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