Binding of β-galactosidase from rat epididymal fluid to the sperm surface by high-affinity sites different from phosphomannosyl receptors
Article
Sosa, MA, Barbieri, MA, Bertini, F. (1991). Binding of β-galactosidase from rat epididymal fluid to the sperm surface by high-affinity sites different from phosphomannosyl receptors
. 93(2), 279-285.
Sosa, MA, Barbieri, MA, Bertini, F. (1991). Binding of β-galactosidase from rat epididymal fluid to the sperm surface by high-affinity sites different from phosphomannosyl receptors
. 93(2), 279-285.
β-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 β-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.
