title: Comparison of receptor properties of erythrocyte membrane glycoproteins.
abstract: Membrane glycoproteins from horse, sheep, goat and bovine erythrocytes were solubilized and purified. These glycoproteins could be placed in three groups based on their degrees of glycosylation: The major bovine erythrocyte glycoprotein (BGII) had 77% sugar, the minor bovine glycoprotein (BGI) had 27% sugar and the others had approximately 50% sugar. Four of the glycoproteins aggregated in a uniform way in aqueous solution--one, BGII, did not. Four had similar subunit sizes of 25-34,000 daltons, but BGII was larger--55,000 daltons. Receptor functions (for plant and invertebrate lectins, antibodies and cell surfaces) of these glycoproteins were primarily those dependent upon the presence of terminal sialic acid residues.
mesh_terms: D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002417:Cattle; D004910:Erythrocyte Membrane / Q000276:immunology*; D004912:Erythrocytes / Q000276:immunology*; D006023:Glycoproteins / Q000276:immunology* / Q000302:isolation & purification; D006041:Goats; D006736:Horses; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000276:immunology*; D008970:Molecular Weight; D011487:Protein Conformation; D011971:Receptors, Immunologic; D012756:Sheep
chemical_list: D002241:Carbohydrates; D006023:Glycoproteins; D008565:Membrane Proteins; D011971:Receptors, Immunologic