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 deuteroproteoses are the primary products of
trypsin-digestion again emphasizes the natural adaptability of this
ferment to the part it has to play in the digestive process. Its
natural function is to take up the work where left by pepsin, and
carry it forward to the necessary point; and hence, when acting
upon a native proteid the primary products of its action correspond
to the secondary products of pepsin-proteolysis. Trypsin is thus
equally efficient in the digestion of all native proteids, but the
products of such action are always deuteroproteoses, peptones, and
crystalline amido-acids. It is to be remembered, however, that in
trypsin-proteolysis the deuteroproteoses and the amphopeptones must
necessarily be represented by bodies in which there is a preponderance
of anti-groups. In pepsin-proteolysis, as we have seen, the hemi- and
anti-groups of the proteid molecule remain more or less united, but in
pancreatic digestion, the formation of amphopeptone is quickly followed
by the breaking down of a portion of the hemipeptone into leucin,
tyrosin, etc. thus leaving a larger proportion of the anti-moiety in
the remaining amphopeptone.
Theoretically, at least, in the-case of a vigorous and long-continued
pancreatic digestion, all of the hemipeptone formed from any native
proteid can be converted into crystalline and other products, thus
leaving a true antipeptone resistant to the further action of trypsin.
Hence, we are prone to speak of the peptone of pancreatic digestion
as antipeptone, although, as can be readily seen, the exact nature of
the peptone, _i. e._, the relative proportion of hemi- and anti-groups
it contains, will obviously depend upon the length of the digestion
and the strength of the ferment. Again, it is possible, as certain
facts seem to suggest, that the amido-acids which are so readily
formed from hemipeptone may come in part directly from the hydration
of a portion of the hemideuteroproteose, without passing through the
preliminary stage of hemipeptone. If so, we have another source of
variation in the relative proportion of hemi- and anti-moieties in the
deuteroproteoses and peptones of pancreatic digestion. Still again, it
is to be remembered that in normal digestive proteolysis, as it occurs
in the living intestinal tract, the proteid matter to be acted upon
has already passed through certain preliminary stages in, its transit
through the stomach, as a result of which still further variations in
the proportion of hemi- and anti-groups may be possible.
Public-domain text, read in full here on John Shaqi.
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