title: Purification and partial characterization of hemagglutinins in seminal plasma of the sea urchin, Hemicentrotus pulcherrimus.
abstract: Two distinct hemagglutinins have been purified from seminal plasma of the sea urchin, Hemicentrotus pulcherrimus. These proteins differ in molecular weight, sugar specificity and trypsin sensitivity. Using SDS-polyacrylamide gel electrophoresis, the molecular weight of both hemagglutinins (HPSPH I and II), was estimated to be about 140 000 and 22 000, respectively. HPSPH I is a glycoprotein, the hemagglutinating activity of which is inhibited by L-arabinose, D-xylose and D-galactose when assayed for rabbit erythrocytes and inhibited by D-galactose, N-acetyl D-galactosamine, L-arabinose and D-xylose for human type A erythrocytes. Inhibitory activity of L-arabinose on agglutination of the human erythrocytes is the same as that of rabbit erythrocytes, although it is much lower than that of D-galactose and N-acetyl D-galactosamine. On the other hand, HPSPH II agglutinates only rabbit erythrocytes and caused fusion of them. Any sugar hitherto examined does not inhibit activities. Both HPSPH I and II are heat-labile and activated by Ca2+. Whereas trypsin, not alpha-chymotrypsin, destroys the former's activity, metaperiodate has not effect upon either.
mesh_terms: D000818:Animals; D002241:Carbohydrates; D004912:Erythrocytes / Q000276:immunology; D006386:Hemagglutination Tests; D006388:Hemagglutinins / Q000302:isolation & purification*; D006801:Humans; D008297:Male; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011817:Rabbits; D012617:Sea Urchins / Q000276:immunology*; D012661:Semen / Q000276:immunology*
chemical_list: D002241:Carbohydrates; D006388:Hemagglutinins; D010446:Peptide Fragments