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Type of Document	Dissertation
Author	Johnson, Kenneth Delford
URN	etd-01152004-161441
Persistent URL	http://resolver.caltech.edu/CaltechETD:etd-01152004-161441
Title	I. The inclusion of monohaptenic substances in immune aggregates. II. Heteroligating antibody in anti-arsanilic acid sera
Degree	PhD
Option	Chemistry
Advisory Committee	Advisor Name Title Dan H. Campbell Committee Chair
Keywords	none
Date of Defense	1954-01-01
Availability	unrestricted
Abstract I Methods have been developed for the preparation and purification of iodinated haptens of the arsanilic acid series suitable for critical experiments on hapten binding in immune aggregates. Additional data are given on the preparation and properties of the solid immune adsorbents described by Lerman. The inclusion of homologous monohaptenic substances in the aggregates formed between these solid adsorbents and homologous antibody has been studied under a variety of experimental conditions. The existence of such hapten binding has been clearly demonstrated, as has the inclusion of hapten in the immune precipitates formed between anti-RBG antibody and both azoprotein and polyhaptenic simple antigens. This demonstration has been interpreted as additional evidence in support of the theory of the bivalence of antibody. II The Pauling theory of antibody synthesis predicts that among the antibody molecules synthesized in spatial contact with the stimulating antigen, there should be some molecules having the two binding sites directed against different antigenic determinants on the surface of the antigen. The existence of such heteroligating antibody molecules has not previously been demonstrated. Data presented here are interpreted as evidence for the existence of heteroligating antibody in the anti-RBG sera studied. These data are derived from experiments on (1) the loss of anti-bovine globulin activity on adsorbing anti-RBG sera with R-adsorbent, (2) the recovery of such activity in the eluates from the adsorbent, and (3) the inclusion of arsanilic acid haptens in precipitates formed between such sera and a native bovine globulin precipitating antigen.
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