Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-35297
Biochim Biophys Acta 1982 Dec 20;7092:220-6. doi: 10.1016/0167-4838(82)90464-2.
Show Gene links Show Anatomy links

Purification and partial characterization of hemagglutinins in seminal plasma of the sea urchin, Hemicentrotus pulcherrimus.

Yamada Y , Aketa K .


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.

PubMed ID: 7150606
Article link: Biochim Biophys Acta


Genes referenced: LOC100887844 LOC594261 srpl