Abstract
Non-precipitating antigen-antibody complexes in sheep anti-terpolypeptide, (Glu 60Ala 30 Tyr 10) n,[GAT], sera have been studied. Antibodies isolated from complezes were found to be precipitable upon re-addition of antigen, hence properties of GAT were examined to determine the nature of non-precipitation. GAT has been shown to be heterogeneous and has been fractionated into molecular wieght fractions with a dispersion from 15,000 to 60,000. Chemical and immunochemical analysis of GAT fractions show: (1) mole %'s of GLU and Ala decrease with increasing mol. wt while Tyr increases and range from 5 to 14 mole %; (2) there is a relationship between the quantity of antibody precipitated at equivalence from anti-GAT sera and mol. wts of fractions; the highest mol. wt precipitates more than twice that of the lowest, while unfractionated GAT precipitates an amount lying midway between these limits; (3) the breadths of the precipitin curves obtained with fractions compared to unfractioned GAT are narrow; and (4) antibody precipitated by the highest mol. wt fraction corresponds with total antibody recoverable from a GAT immunoadsorbant. Precipitin analysis with a high mol. wt fraction, on sera spent of antibody precipitabler by a low mol. wt fraction suggest that antigenic determinants of GAT occuring at high and low degrees of polymerization are independent, yet inhibition experiments indicated that these determinants are related. These results are consisten with the notion that in addition to mol. wt heterogeneity in GAT, there is a novel kind of antigenic arrangement on GAT molecules such that determinants occur on GAT molecules in a sequential fashion. This combination can account for broad precipitin curves observed with unfractioned GAR and the existence of soluble complexes at equivalence. This notion may also be a clue to the kinds of antigens capable of inducing soluble complex diseases, and in conjunction with the immune response to GAT, indicates than an animal can simultaneously produce antibodies to a vast number of related antigenic determinants and do so with an elegant of specificity.
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