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
It is thus evident that a certain amount of urea may come from the more
or less direct hydrolysis of proteid matter in the intestinal canal,
all but the last steps in the process being the result of the ordinary
cleavage processes incidental to trypsin-proteolysis. This fact affords
additional evidence of the profound changes set in motion by this
proteolytic enzyme. It is not, of course, to be understood that all the
urea formed in the body has its origin in this manner. Such a method of
decomposition taking place in the intestinal tract would be exceedingly
unphysiological and wasteful, but we can readily see how such a line of
cleavage might result in inestimable gain to the economy in cases where
excess of proteid food has been ingested. Under such circumstances, a
portion of the surplus might be broken down directly in the intestine
into this urea-antecedent, and thus quickly removed from the system
with a minimum amount of effort on the part of the economy. Drechsel
estimates that about one-ninth of the urea daily excreted may come from
the direct decomposition of lysatin, the latter obviously having its
origin in trypsin-proteolysis.
Another product of trypsin-proteolysis which has long been recognized,
although its real nature has not been known, is tryptophan or
proteinochromogen. This body is not only a product of the pancreatic
digestion of proteids, but it is also formed whenever native proteids
are broken down through any influence whatever, the substance coming
presumably from the hemi-moiety of the molecule. It is especially
characterized by the bright-colored compound it forms with either
chlorine or bromine, so that for a long time it went by the mystical
name of the “bromine body.” When brought in contact with either of
these agents, it immediately combines with them to form a new compound
of an intense violet color, termed proteinochrome. This constitutes
the usual test for its presence, a little bromine water, for example,
quickly bringing out a violet color when added to a fluid containing
the chromogen. The body is readily soluble in alcohol, and hence can
be easily separated from the primary products of trypsin-proteolysis,
such as the proteoses and peptones. Krukenberg considered the substance
not a true proteid, but rather a body belonging to the indigo-group;
but Stadelmann, who has given the matter a very thorough investigation,
comes to the conclusion that it is truly a proteid body, in part
closely related to peptone, although in many ways quite different.
The following composition of bromine proteinochrome, as determined by
Stadelmann,[190] shows the general nature of the compound formed when
bromine combines with the chromogen:
_A_ _D_
C 49.00 48.12
H 5.28 5.09
N 10.99 11.92
S 3.77 3.10
O 11.01 12.00
Br 19.95 19.77
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