Isolation and partial characterization of the major glycoproteins of horse and swine erythrocyte membranes.
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.
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
D000596:Amino Acids; D006023:Glycoproteins