HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Forster, O. Articles by Weigle, W. O. Search for Related Content PubMed PubMed Citation Articles by Forster, O. Articles by Weigle, W. O. Pubmed/NCBI databases Substance via MeSH Medline Plus Health Information Dietary Proteins

The Formation of Soluble Complexes in the Region of Antibody Excess with Protein Antigens and Their Rabbit Antibodies¹

From the Division of Experimental Pathology, Scripps Clinic and Research Foundation, 476 Prospect Street, La Jolla, California

Abstract

Using the technique of Nisonoff and Winkler of slow addition of antigen to antibody under vigorous mixing, the formation of soluble complexes in antibody excess have been studied with egg albumin, bovine serum albumin and bovine -globulin. With all three systems the formation of soluble antibody excess complexes was possible, although the antibody concentrations required increased with the molecular weights of the antigens.

Thorough mixing seemed to be of primary importance in order to maintain a high antibody excess at the site of reaction. The time of addition may be relatively short without impairing the result, whereas stirring over a prolonged period leads to denaturation of the antibody and to increased precipitation.

The formation of the complexes can be inhibited, and preformed complexes can be precipitated by a heat labile factor present in the euglobulin fraction of fresh guinea pig serum and rabbit serum. This factor is probably complement-nitrogen. The composition of the complexes was determined using fresh guinea pig serum for precipitation of complexes formed with I¹³¹ labeled EA and I¹²⁵ labeled anti-EA. The antibody: antigen ratio found was higher than the initial combining ratio.

Footnotes

¹ This is Publication 27 from the Division of Experimental Pathology, Scripps Clinic and Research Foundation.

This work was supported by U.S.P.H.S. grants and an Atomic Energy Commission Contract.

Presented in part at the meeting of the American Society of Immunology, Atlantic City, New Jersey, April 13–18, 1962.

² Foreign Research of the National Institutes of Health, U.S.P.H.S. Present address: Department of Experimental Pathology, University of Vienna, Austria.

³ This work was performed during the tenure of a U.S.P.H.S. Research Career Award.