title: Saccharide-binding properties of boar AQN spermadhesins and DQH sperm surface protein.
abstract: Heparin-binding proteins BHB 2-BHB 5 were purified from boar seminal plasma by affinity chromatography on a heparin-polyacrylamide column and reversed phase HPLC. Three of the proteins, BHB 3-BHB 5, were found to be identical to spermadhesins AQN 1-AQN 3 isolated from boar spermatozoa. The lectin-like properties of the isolated proteins BHB 2-BHB 5 were studied using double-diffusion in agarose gel, enzyme-linked binding assay, and inhibition assays of erythroagglutinating activity. It was found that proteins BHB 3-BHB 5 (spermadhesins AQN 1-AQN 3) interacted with glycoproteins containing O-glycosidically bound oligosaccharide chains, but not with those containing only N-linked carbohydrate chains. The strongest interaction was observed between BHB 3 (AQN 1) and desialyzed bovine submaxillary gland mucin, the glycoprotein containing only O-glycosidically linked saccharides. No interaction of BHB 3-BHB 5 proteins with simple saccharides, their derivatives or acidic polysaccharides was observed. Both the hemagglutinating activity and saccharide-binding properties of BHB 2 protein were quite different. Agglutinating activity of human erythrocytes by BHB 2 protein was significantly higher than that by BHB 3-BHB 5 proteins (AQN spermadhesins). In contrast to AQN spermadhesins, BHB 2 protein (DQH sperm surface protein) interacted strongly with acidic polysaccharides and sialyzed glycoproteins, but no binding of desialyzed glycoproteins as well as N-acetyl-alpha-D-galactosaminyl-O-serine,simple monosaccharides and amino sugars was observed.
authors.affiliation: Department of Biochemistry, Charles University, Prague, Czech Republic.
authors.forename: M
authors.initials: M
authors.lastname: Tichá
authors.forename: M
authors.initials: M
authors.lastname: Kraus
authors.forename: D
authors.initials: D
authors.lastname: Cechová
authors.forename: V
authors.initials: V
authors.lastname: Jonáková
mesh_terms: D000818:Animals; D050260:Carbohydrate Metabolism; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002417:Cattle; D015815:Cell Adhesion Molecules / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D006384:Hemagglutination; D006801:Humans; D066298:In Vitro Techniques; D008297:Male; D008562:Membrane Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding; D012661:Semen / Q000378:metabolism; D029589:Seminal Plasma Proteins; D013084:Sperm-Ovum Interactions; D013094:Spermatozoa / Q000378:metabolism*; D013552:Swine; D015044:Zona Pellucida / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; D008562:Membrane Glycoproteins; D029589:Seminal Plasma Proteins; C121098:BSP1 protein, Sus scrofa; C425042:spermadhesin