Separation of H‐Activity from Isolated Glycoproteins of Human O Erythrocyte Membranes

Abstract

Abstract. H activity can be dissociated from human erythrocyte membrane glycoproteins prepared from OMM or ONN erythrocytes utilizing Phaseolus vulgaris phytohemagglutinin coupled to Sepharose 4B or by precipitation of the glycoproteins with soluble phytohemagglutinin. The three glycoprotein components of the erythrocyte membrane, as resolved by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, bind specifically to phytohemagglutinin. Although such glycoproteins no longer exhibit H activity, they do retain M or N activity. H activity can be recovered in a fraction that does not bind to phytohemagglutinin coupled to Sepharose or to soluble phytohemagglutinin, contains no detectable glycoprotein components, and binds to Ulex lectin coupled to Sepharose.