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J. Biol. Chem., Vol. 260, Issue 5, 2715-2718, Mar, 1985

Purification of the Mr 80,000 and Mr 210,000 proteins of the sea urchin sperm plasma membrane. Evidence that the Mr 210,000 protein interacts with egg jelly

SB Podell and VD Vacquier

Two immunologically cross-reactive plasma membrane proteins, of Mr 80,000 and Mr 210,000, have been purified to apparent homogeneity from sperm of the sea urchin Strongylocentrotus purpuratus. Purification includes a combination of antibody and wheat germ agglutinin affinity chromatography. The two proteins have similar but not identical amino acid compositions; however, their carbohydrate composition differs substantially. After purification, the Mr 210,000 protein binds to both living eggs and isolated egg jelly in a species-specific manner, but the Mr 80,000 protein does not. The inactivity of the Mr 80,000 protein could be due to denaturation during purification. The data are consistent with a model in which the Mr 210,000 protein acts as a jelly receptor in the sperm membrane, promoting the ion movements necessary to initiate the sperm acrosome reaction.
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				K. J. Mengerink and V. D. Vacquier An ATP-binding Cassette Transporter Is a Major Glycoprotein of Sea Urchin Sperm Membranes J. Biol. Chem., October 18, 2002; 277(43): 40729 - 40734. [Abstract] [Full Text] [PDF]