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Mouse sperm bound to egg zona pellucida and attached to unfixed rabbit erythrocytes specifically, but not to fixed-erythrocytes. When mouse sperm were treated with ionophore A23187, the sperm lost both the binding ability to the zona pellucida and the attachment ability to rabbit erythrocytes. The membrane vesicles released from A23187-treated sperm agglutinated rabbit unfixed erythrocytes. Sperm binding to egg zona pellucida was also inhibited by the membrane vesicles. The inhibition spectrum of a hemagglutination and of an inhibitory activity of sperm-egg binding by various carbohydrates was studied. The hemagglutination was inhibited by N-acetyl-glucosamine, N-acetylgalactosamine and glyco-proteins, such as fetuin and orosomucoid, but not by N-acetylneuraminic acid (NeuNAc) in saccharides and asialo-transferrin in glycoproteins. On the other hand, the sperm-egg binding was inhibited most effectively by NeuNAc and also by asialo-transferrin. The inhibition spectrum of hemagglutination and sperm-egg binding didn't agree with each other. These results suggest that a lectin-like molecule is expressed on mouse sperm surface but is not directly concerned in sperm-egg binding.

Studies on Mouse Sperm Lectin; The Existence and The Participation in Sperm-Egg Binding.