Abstract
Summary
Human erythrocyte membrane glycoproteins were extracted by the chloro-form-methanol (CM) and the lithium diio-dosalicylate-phenol (LIS) methods. Each preparation comprised up to 50% protein and 30-40% carbohydrate (reducing sugar and N-acetylneuraminic acid). Both types of preparations contained receptors for influenza virus.
Electrophoretic analysis in SDS polyacryl-amide gel in a phosphate buffer system revealed one major and one minor band in both preparations. In contrast, numerous interconvertible bands, including PAS 1,2,3 and 4 were found in gels using a Tris/glycine buffer system. The major glycoprotein (PAS-1) was separated from other CM glycoprotein components by preparative electrophoresis.
Antisera made to both CM and LIS glycoproteins elicited agglutinins which were equally reactive with cells of all three ABO(H) blood groups and unrelated to the corresponding blood group determinants. PAS-1 also evoked similar broadly specific antibodies which, in quantitative precipitin analyses and two dimensional immunoelectrophoresis, served to establish antigenic identity among CM and LIS glycoproteins, probably based on common determinants in the protein moiety.
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