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Partial Purification and Characterization of Schistosoma Mansoni Soluble Egg Antigen with Con A-Sepharose Chromatography¹

From the Departments of General Biology and Microbiology, Vanderbilt University, and the Veterans Administration Hospital, Nashville, Tennessee 37235

Abstract

A crude preparation of Schistosoma mansoni soluble egg antigen (SEA) was subjected to affinity chromatography with concanavalin A (Con A) bound to Sepharose 4B. The resulting Con A fractions (bound and unbound) were characterized with sodium dodecyl sulfate (SDS) gel electrophoresis, immunoelectrophoresis, immunodiffusion, and lymphocyte blastogenesis techniques. In the fraction that did not bind to Con A there were at least two distinct antigens, and there were also at least two distinct antigens in the fractions that did bind to Con A. With SDS polyacrylamide gel electrophoresis, at least 20 distinct protein bands (Coomassie blue staining) and three glycoprotein bands (PAS reactive) were present in the unbound fractions from Con A chromatography. The bound fractions separated into at least six distinct glycoproteins with SDS electrophoresis. Although both the bound and unbound fractions contained precipitating antigens, only the bound fractions were capable of eliciting lymphocyte blastogenic responses.

Footnotes

¹ This work was primarily supported by the United States-Japan Cooperative Medical Science Program through National Institute of Allergy and Infectious Diseases, National Institutes of Health, Public Health Service Grant AI 12996 and in part by Public Health Service Grant AI 11289 and the Medical Research Service of the Veterans Administration.