Abstract
Our previous immunological studies 1 with the split products of casein and a compound of casein with protamin, which were undertaken for the purpose of gaining some insight as to the nature of biological specificity have apparently been fruitless in so far as the main point at issue was concerned, with one exception. In our comparative studies of the antigenic properties of split paranuclein with paranuclein synthesized by the reversible action of pepsin from the products of peptic digestion, we were apparently able to demonstrate the genesis of an antigenic property.
The present study deals with the investigation of the antigenic properties of our second compound of casein with a non-antigenic protein, globin caseinate. We find that globin is non-antigenic and highly toxic, producing in guinea-pigs the typical symptoms and lesions of anaphylaxis. When compounded with casein, it still remains slightly toxic. An anti-serum derived by repeated injections of rabbits with globin caseinate contains fixation bodies for casein, globin caseinate, and, curiously enough, for globin, although globin alone does not produce such antibodies. By absorption experiments it may be shown that the antibodies in anti-globin caseinate serum are two in number, one for casein and one for globin. Thus it appears that the change in globin brought about by this combination with casein renders it antigenic.
A further study of similar and of more complex compounded proteins should give further insight as to the nature of specificity.
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