Competition between seminal and exogenous proteinase inhibitors for sites on murine epididymal sperm.
Sixteen proteinase inhibitors were tested for their ability to compete with the natural seminal inhibitor for binding to the surface of murine epididymal sperm. The most effective competitors, 4-methylumbelliferyl-p-quanidinobenzoate (MUGB) and p-nitrophenyl-p-guanidinobenzoate (NPGB), are also effective inhibitors of both murine acrosin and in vitro fertilization of mouse gametes. The data support the suggestion that the inhibition of fertilization by these inhibitors may be effected by their action on the sperm surface rather than binding to enzymes located within the acrosome. Since the surface acceptor molecule recognizes a number of inhibitor types, as well as substrates for such enzymes as trypsin and acrosin, the acceptor's binding site may be similar to the active site on the enzyme.
D000818:Animals; D001667:Binding, Competitive; D004822:Epididymis / Q000201:enzymology*; D005306:Fertilization; D008297:Male; D051379:Mice; D008813:Mice, Inbred ICR; D011480:Protease Inhibitors / Q000378:metabolism*; D012661:Semen / Q000201:enzymology*; D013075:Sperm Capacitation; D013094:Spermatozoa / Q000201:enzymology*
D011480:Protease Inhibitors