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
With relatively large amounts of proteid, we may have half or even
quarter saturated proteid molecules, in which the weakness of the
combined acid is far more pronounced than in the case of the fully
saturated molecule. Such a condition of things must obviously exist
in the early stages of gastric digestion. With an excess of proteid
matter in the stomach, some time must elapse before the secretion
of hydrochloric acid will be sufficient to furnish acid for all of
the proteid matter present, yet pepsin-proteolysis does not wait the
appearance of free acid. Indeed, the proteid matter may not have
combined with more than half its complement of hydrochloric acid before
digestive proteolysis is well under way. I have made many analyses of
the stomach-contents after test meals, and under other conditions,
where no free acid could be detected by the tropaeolin test, or better,
by Günzburg’s reagent (phloroglucin-vanillin), although phenolphthalein
as well as litmus showed strong acid reaction, and yet not only could
acid-albumin be detected in the filtered fluid, but likewise proteoses
and peptones. In other words, pepsin-proteolysis can proceed in the
absence of free hydrochloric acid, although not at the same pace.
Hence, proteoses and even peptones may make their appearance in the
stomach-contents at a very early period of digestion, _i. e._, the
final products of proteolysis may be found in a mixture containing even
a large proportion of wholly unaltered proteid, and obviously at an
early stage in the process. Expressed in other language, a portion of
the first formed acid-albumin or syntonin may be carried forward by the
digestive process to the secondary proteose and peptone stage, before
the larger portion of the ingested proteid food has even combined with
sufficient acid to insure the complete formation of acid-albumin.
This introduces another factor, to be referred to later on, viz.,
the relative combining power of different forms of proteid matter,
especially the proteoses and peptones, as contrasted with native
proteids.
In proof of the statement that pepsin-proteolysis can proceed in the
absence of free hydrochloric acid, provided combined acid be present,
allow me to cite one or two experiments bearing on this point. A
perfectly neutral solution of egg-albumen, containing 0.8169 gramme
of ash-free albumin per 10 c.c. of fluid, was employed as the proteid
material. In order to completely saturate the proteid contained in
20 c.c. of this neutral albumen solution, 50 c.c. of 0.2 per cent. HCl
were required. Two mixtures were then prepared as follows:
_A._ Twenty c.c. of the neutral albumen solution + 50 c.c. 0.2 per
cent. HCl + 30 c.c. of a weak aqueous solution of pepsin, perfectly
neutral to litmus. This mixture gave only the faintest tinge of a
reaction for free acid when tested by Günzburg’s reagent.
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