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Studies on Human Secretory Immunoglobulin A

VI. Cyanogen Bromide Cleavage¹

From the Institute of Dental Research, Departments of Microbiology and Medicine, University of Alabama in Birmingham, Birmingham, Alabama 35294

Abstract

Fragments produced by cyanogen bromide cleavage of human secretory IgA were fractionated before and after the splitting of disulfide bonds on Sephadex G-200 columns in 5 M guanidine · HCl. By electrophoretic, antigenic, amino acid, and carbohydrate analyses of individual fractions it was revealed that J chain was released as a result of cyanogen bromide cleavage. Secretory component remained associated with a large fragment(s) of chain (approximately 80% the size of the original chain) to which L chains were also linked. Data indicate that J chain and secretory component are linked to different cyanogen bromide fragments of the chain(s) and are not mutually connected by disulfude bonds. Although J chain might mediate the binding of secretory component through a disulfide-bond interchange reaction, the J chain is not involved in direct bridging between secretory component and polymeric IgA molecules.

Footnotes

¹ This investigation was supported by United States Public Health Service Grants AI-10854 and DE 02670.