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The Journal of Immunology, 1962, 89: 367-376.
Copyright © 1962 by The American Association of Immunologists, Inc.
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Increased Precipitability of Antibody as a Result of Iodination1

David Pressman and Gerald Radzimski

From the Department of Biochemistry Research, Roswell Park Memorial Institute, New York State Department of Health, Buffalo, New York

Abstract

The precipitability of anti-p-azobenzoate antibody by an antigen containing azobenzoate groups is not complete and soluble complexes of antigen-antibody are present in the supernatant. A limited degree of iodination of the antibody increases its precipitability by antigen. Extensive iodination causes decreased precipitation presumably through effect on the binding site itself. The increase in precipitability is explained on the basis of increased hydrophobic bonding, or increased van der Waals' interaction due to the added iodine atom or denaturation.

The use of chemically altered antibody systems is proposed for a study of the effect of alteration on protein-protein interactions in aqueous systems. The precipitability of antiprotein antibody such as anti-BSA or antibovine {gamma}-globulin antibodies is markedly decreased at levels of iodination which give increased precipitation with antihapten antibody. It would appear that the antiprotein antibody site is more sensitive to iodination than antihapten antibody sites. This may be due to presence of a particularly important and sensitive group in the site or due to the presence of more than one iodinatable group in the site, any one of which when iodinated destroys ability of the site to combine with antigen.

Footnotes

1 Supported in part by the National Institute of Allergy and Infectious Disease, U. S. Public Health Service Grant E-2342.






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