PREPARATION OF AN INHIBITOR OF VIRAL HEMAGGLUTINATION FROM HUMAN ERYTHROCYTES

Abstract
By manipulation of pH, hot phenolic extraction, chloroform-methanol treatment, and ultracentrifugation, a highly potent inhibitor of viral hemagglutination was obtained from human erythrocyte stroma. The inhibitor appears to be a glycoprotein containing 22-24% sialic acid, 12% hexose, 12% hexosamine, 1% fucose, and at least 11 amino acids. Sialic acid occupies a terminal position. The molecular weight is approximately 15,000. M and N blood group activity are associated with the protein.