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Isolation of Human C4 by Affinity Chromatography with IgG-Coupled Sepharose 6B

Department of Microbiology and Public Health, Michigan State University, East Lansing, Mich. 48823

Abstract

At least four examples exist which demonstrate an association of C4 with serum proteins. It has been previously reported that C4 forms association products with itself and with human 7S -globulin in the presence of C1. Native C4 is known to complex with C2 in a reversible fashion. This reversible association of C2 and C4 is converted to a firm complex which is due to the proteolytic action of C1. Finally, C4 is believed to react with receptor sites on antibody molecules as well as erythrocyte membrane receptors during immune hemolysis.

Human IgG was covalently linked to Sepharose 6B under basic conditions by use of cyanogen bromide. The resultant Sepharosecoupled IgG was stored at 4°C with 0.005% sodium azide until ready for use. Approximately 1 mg of IgG was bound per 20 mg Sepharose. Crude C4 from a pseudoglobulin fraction of human serum and subsequently eluted from DEAE-cellulose at pH 7.3 was used for studies with insoluble IgG.