The isolation and characterization of a concanavalin A receptor from boar spermatozoa surface.
Boar spermatozoa were radioactively labeled by either lactoperoxidase-catalysed iodination or galactose oxidase oxidation followed by reduction with tritiated sodium borohydride. Plasma membrane glycoproteins were solubilized with the non-ionic detergent Nonidet P40 and separated by affinity chromatography on concanavalin A-Sepharose. A major water-soluble concanavalin A receptor of molecular weight greater than 160 000 was isolated by gel filtration and ion-exchange chromatography. Its amino acid and carbohydrate composition were determined. This glycoprotein is susceptible to digestion by trypsin or chymotrypsin.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002462:Cell Membrane / Q000276:immunology; D003208:Concanavalin A / Q000276:immunology*; D008297:Male; D008970:Molecular Weight; D011952:Receptors, Concanavalin A / Q000302:isolation & purification / Q000378:metabolism*; D013094:Spermatozoa / Q000276:immunology*; D013552:Swine
D000596:Amino Acids; D002241:Carbohydrates; D011952:Receptors, Concanavalin A; D003208:Concanavalin A