The Molecular Biology of Fertilization by Heide Schatten

By Heide Schatten

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In control experiments, identical concentrations of bovine serum albumin have no effect on sperm-egg binding, and heat denaturing the α-lactalbumin destroys its ability to modify GalTase activity and to inhibit sperm-zona binding (Shur and Hall, 1982b). GalTases are readily inhibited by the substrate analog, UDP-dialdehyde, which forms Schiffs bases in the UDPGal-binding site (Powell and Brew, 1976). UDP-dialdehyde inhibits sperm surface GalTase activity and sperm binding to the zona pellucida to identical degrees, and in a dose-dependent manner.

2. Receptors and Membrane Interactions Fig. 4. 27 T r a n s m i s s i o n e l e c t r o n m i c r o g r a p h of s p e r m and egg binding. Our laboratory has been involved in the isolation and characterization of the egg cell surface receptor that mediates the interaction of the egg with sperm bindin. , 1977). , 1984). In several respects, however, it proved to be unlike previously described receptors for soluble protein ligands. The isolated sperm receptor is insoluble in most solvents and is a high-molecular-weight glycoconjugate 7 (>10 ).

Most glycosyltransferase activities are membrane bound, but some activities have been identified in a variety of body fluids and cultured cell secretions. However, the function of soluble or secreted glycosyltransferase activities, other than that found in milk, is unknown. Glycosyltransferases synthesize complex glycoconjugates by the addition of the appropriate monosaccharide residue donated from sugar nucleotide substrates to the nonreducing terminus of the growing polysaccharide chain (Schachter and Roseman, 1980).

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