title: Heterogeneity of aggregates of the human erythrocyte membrane glycoproteins.
abstract: The crude red cell glycoproteins obtained by four different methods are compared. The most selective isolation of the major membrane glycoprotein (MN blood group glycoprotein) is achieved by the phenol-water extraction procedure. A different degree of aggregation of this glycoprotein in water and in various buffers is demonstrated. The gel filtration of the crude glycoprotein on a Sepharose 4B column in 0.05 M pyridine--acetate buffer of pH 5.3 gives four fractions with different chemical compostition and serologic properties. The fractions obtained are heterogenous in SDS-PAGE and represent different kinds of glycoprotein aggregates. The distribution of serologic activities in the fractions obtained indicates that A, B and I activities found in the crude prepration of red cell glycoprotein are not connected with MN glycoprotein.
mesh_terms: D000017:ABO Blood-Group System; D000596:Amino Acids / Q000032:analysis; D001789:Blood Group Antigens; D002241:Carbohydrates / Q000097:blood; D004910:Erythrocyte Membrane / Q000032:analysis*; D004912:Erythrocytes / Q000032:analysis*; D006023:Glycoproteins / Q000097:blood*; D006801:Humans; D007048:I Blood-Group System; D008951:MNSs Blood-Group System; D008565:Membrane Proteins / Q000097:blood*; D011485:Protein Binding
chemical_list: D000017:ABO Blood-Group System; D000596:Amino Acids; D001789:Blood Group Antigens; D002241:Carbohydrates; D006023:Glycoproteins; D007048:I Blood-Group System; D008951:MNSs Blood-Group System; D008565:Membrane Proteins