The nutrition of manChittenden, R. H. (Russell Henry)
Science
The nutrition of man
Chittenden, R. H. (Russell Henry)
Nutrition
The proteid molecule is presumably built up of amino-acids variously
joined together, this synthesis being accomplished, doubtless, by the
condensation of different types of amino-acids, in which the first
of the above groups represents the more common method of union. We
may indeed conjecture that such methods of condensation take place in
the human body, in the epithelial cells of the intestine, and in the
tissues in general; and that by such methods, construction of proteid
is accomplished out of the various fragments split off by digestion,
etc. In a tentative way, the principle may be illustrated by the fusion
of leucin and glutaminic acid,--following Hofmeister’s suggestion,--in
which a still larger complex is formed:
: :
--CO-:-NH--CH--CO--NH--CH--CO-:-NH--
: | | :
C_{4}H_{9} (CH_{2})_{2}
|
CO·OH
Leucin Glutaminic acid
In this way, step by step, the proteid molecule is built up, and
naturally in katabolism the proteid breaks down along certain definite
lines of cleavage, with formation of katabolic products containing
those groups, or chemical nuclei, which characterize the different
proteid molecules. For it is to be clearly understood that there are
many different forms of proteid, perhaps superficially alike, but
possessed of physiological individuality. This is well illustrated
by the two primary proteoses formed in digestion. As will be
recalled, there are at first two proteoses produced, protoproteose
and heteroproteose. These are, superficially at least, not radically
unlike; they possess essentially the same percentage composition, but
when broken down by vigorous chemical methods they show a totally
different make-up. In other words, at the very beginning of digestion
there is a splitting up of the proteid into two parts, which have
quite a different chemical structure, as is clearly indicated by the
difference in the character and amount of the decomposition products
yielded by hydrolytic cleavage. Thus, heteroalbumose as derived from
blood-fibrin contains 39 per cent of its total nitrogen in basic form,
_i. e._, in a form which goes over into the basic bodies, arginin,
lysin, and histidin, etc. On the other hand, protoalbumose from the
same source yields hardly 25 per cent of basic nitrogen. Further,
heteroalbumose yields only a very small amount of tyrosin, while
protoalbumose gives on decomposition a large amount of this substance.
Again, heteroalbumose furnishes a large yield of leucin and glycocoll,
while protoalbumose gives no glycocoll and only a little leucin.
Obviously, these two proteoses have an inner structure quite divergent
one from the other, and owing to this fact they must play a quite
different rôle in metabolism.
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