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beta-Galactosidase, known to be secreted by epithelial cells lining the rat epididymal duct, binds to the surface of spermatozoa from the caudal region with high affinity and in a saturable form. The binding was not inhibited by mannose-6-phosphate, but was inhibited by fructose phosphate derivatives, a peculiarity previously demonstrated for the membranes of epididymal tissue. Fructose phosphate derivatives released 55% of beta-galactosidase activity from the spermatozoa. These results suggest that in the epididymis there is a special transport system for hydrolases, which could be involved in the secretion of enzymes destined for spermatozoa. This transport would require receptors that recognize sugar ligands other than mannose-6-phosphate. These receptors were present in the epididymal tissue and on the sperm surface.

Binding of -galactosidase from rat epididymal fluid to the sperm surface by high-affinity sites different from phosphomannosyl receptors