title: Isolation and partial characterization of the major glycoproteins of horse and swine erythrocyte membranes.
abstract: The major glycoproteins of horse and swine erythrocyte membranes were isolated and examined chemically and immunologically. The major glycoprotein of horse erythrocyte membranes had a molecular weight of 33 000 and consisted of 46.2% protein and 53.8% carbohydrate, of which 9.4% was hexose, 10.1% hexosamine and 33.7% sialic acid. This glycoprotein was associated with activity for the infectious mononucleosis heterophile antigen. There were two different major glycoproteins in swine erythrocyte membranes. One major glycoprotein had a molecular weight of 46 200 and consisted of 34.2% protein and 65.8% carbohydrate, of which 18% was hexose, 19% hexosamine and 27.2% sialic acid. This glycoprotein had phytohemagglutinin (Phaseolus vulgaris) binding activity. The other glycoprotein had a molecular weight of 29 000 and consisted of 50.4% protein and 49.6% carbohydrate, of which 6.4% was hexose, 7.0% hexosamine and 36.3% sialic acid. This glycoprotein had weak or absent phytohemagglutinin binding activity.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002462:Cell Membrane / Q000032:analysis*; D004912:Erythrocytes / Q000032:analysis*; D006023:Glycoproteins / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D006736:Horses; D008970:Molecular Weight; D013552:Swine; D013961:Thyroid Gland / Q000502:physiology
chemical_list: D000596:Amino Acids; D006023:Glycoproteins