By E. R. Gold and D. B. Peacock (Auth.)
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If monomers of say 20 D,L-alanine residues are then added to the short side-chains the polymer again becomes non-antigenic, probably because the tyrosine-glutamic acid peptides are now masked. If the experiment is repeated in a different order so that alanine monomers are first added to a polylysine backbone to yield a branched structure, the molecule is again non-antigenic, even though molecular weights of 20,000-200,000 can be achieved. The addition of tyrosine and glutamic acid to this structure will again result in an antigenic molecule, even when the chemical content of the final molecules in the first and second experi ments is identical.
Mostly they make very good antigens. It is now appreciated that carbohydrates certainly and lipids possibly are antigenic, but they are both more con cerned in specificity and will be discussed under that heading. The amino-acid spectrum of many proteins has been investigated and it has been shown that several non-aromatic amino-acids are inessential for antigenicity. As we have seen, treatment of albumin with alkalis destroys its anti genicity, but can be restored by nitration of the denatured protein.
The crux of the matter would seem to be that it is not so much a terminal or subterminal position in a polypeptide chain that decides whether a sequence of amino-acids acts as a determinant, but rather the position of a sequence with respect to the molecule as a whole. In other words, in serological reactions with native protein it is the accessibility of a deter minant on the surface of the molecule that is of primary importance. 8. SIZE OF DETERMINANTS Progress in the field of protein chemistry is now extremely rapid.