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Immunoglobulins of the Rhesus Monkey (Macaca Mulatta)

III. Structure and Activity of Rhesus IgG and IgM Antibodies Synthesized in the Primary Response and in the Hyperimmune State¹

From the Departments of Microbiology and Medicine, Northwestern University School of Medicine, Chicago, Illinois

Abstract

Rhesus monkey IgG and IgM preparations containing anti-bovine serum albumin (BSA) antibody were chromatographically separated from pooled hyperimmune serum, and IgM anti-BSA was separated from pooled sera drawn during the early primary response (IgM-p). Exposure of the antibody preparations to 0.1 M 2-mercaptoethanol did not markedly reduce the antibody activity in passive hemagglutination of the IgG or hyperimmune IgM (IgM-h) preparations. The hemagglutinating activity of IgM-p was completely destroyed. Alkylation of the reduced IgM-h molecules with iodoacetamide did not reduce the hemagglutinating activity of the mercaptoethanol-treated antibody. Analytical Sephadex chromatography and sucrose density gradient ultracentrifugation of reduced and alkylated IgM-h demonstrated that the 18 S macroglobulin had been degraded to subunits possessing antibody activity. These subunits were demonstrated to have a sedimentation coefficient of 8.0 S and a molecular weight of approximately 190,000. IgM-h anti-BSA stored at 4°C for 3 months was, in part, spontaneously reduced to 8.0 S subunits which retained antibody activity in passive hemagglutination. However, the total hemagglutinating activity of IgM-h significantly decreased during prolonged storage at 4°C.

Footnotes

This work was supported in part by the Ernest S. Bazley Asthma Research Fund to Chicago Wesley Memorial Hospital, Chicago, Illinois.

² University Post-Doctoral Scholar of the Medical Scientist Training Program, National Institutes of Health, United States Public Health Service No. 5-T5-GM01671-03.

³ Ernest S. Bazley Professor of Allergy and Immunology.