Abstract
Abstract Oxidative sulfitolysis as a method for disruption of disulfide bonds was first applied to proteins by Swan (1). More recently this method has been used with immunoglobulins (2). In the present study oxidative sulfitolysis of IgM, followed by chromatography in 5 M guanidine HCl, resulted in high yields of H and L chains. Quantitative data provided additional evidence for the four-chain model of IgM subunits consisting of two H and two L chains. Determination of disulfide bonds and cysteic acid residues indicated disruption of three interchain disulfide bonds per H chain, mutually connecting H chains, and one other disulfide bond connecting H and L chains. The H chain was found to contain five and the L chain two intrachain disulfide bonds. In comparison with reduction and alkylation, oxidative sulfitolysis has the advantage of producing no side reactions and of providing highly soluble chains. Materials and Methods. Waldenström's IgM (Dau) was prepared as described previously (3).
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