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The Dissociation of Human Serum 7S and Bovine Colostrum Immune Globulins into Subunits by Reduction-Alkylation-Succinylation¹

Biochemistry Department, Presbyterian-St. Luke's Hospital and the Department of Biological Chemistry, University of Illinois, College of Medicine, Chicago, Illinois 60612

Abstract

Human 7S and bovine colostral immunoglobulins were succinylated and reduced-alkylated, and their subunits were separated by chromatography on Sephadex G-200 columns. Human 7S immunoglobulin yielded heavy chains with a molecular weight of 55,700 and light chains with a molecular weight of 22,300. Bovine colostral immunoglobulins gave heavy and light chains with molecular weights of 49,500 and 25,200, respectively. Since the molecular weight of the colostral immunoglobulin of 166,000 is not accounted for by two heavy and two light chains, the possibility is raised that another subunit possibly exists in colostral immunoglobulin. The succinylated proteins lost their ability to form precipitin lines with antisera to native bovine and human immunoglobulins, but they formed precipitin lines in the double diffusion system with an antiserum to the succinyl hapten residues.

Footnotes

This work was supported by United States Public Health Service Grant GM-11985-06.

² United States Public Health Service Trainee, Grant 5 T01 GM 00471-08 BCH. Portions of this work are taken from a thesis to be presented by Rainer Zschoche in partial fulfillment of requirements for the degree of Doctor of Philosophy in Biological Chemistry from the University of Illinois, College of Medicine, Chicago, Illinois.