Abstract
Purification of the envelope antigen of Yersinia pestis EV with passive hemagglutination activity is described. The purification procedure consisted of pancreatin digestion, chromatography on human erythrocyte stroma set on Celite, and rechromatography on Sephadex G-200. Chemical, physical, and biological properties of this antigen were investigated. The results show the lipid-polysaccharide structure of the isolated antigen. The carbohydrate moiety of the galactolipid antigen consists of galactose and fucose. The lipid fraction contained phosphatidylethanolamine and phosphatidylserine. The preparation showed high specificity in the hemagglutination reaction and in Y. pestis phage receptor activity. In two-dimensional immunoelectrophoresis, the isolated pancreatic envelope digest antigen appeared as a single line. Two-dimensional immunoelectrophoresis was modified for tandem separation and was employed to electrophoretically identify the pancreatic envelope digest, trypsin envelope digest preparation, and F1 envelope antigen of Y. pestis. Related or identical antigens showed confluence of peaks with reactions of identity.
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