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Research note: kinetic and inhibition studies with turkey acrosin
M E Richardson1, N Korn, A B Bodine
1Department of Animal, Dairy, and Veterinary Sciences, Clemson University, South Carolina 29634.
Poultry Science
|October 1, 1992
Abstract:
Acrosin was extracted from turkey spermatozoa and partially purified by chromatofocusing. Enzyme activity was tested over a pH range with three different substrates. In each case, the pH optimum was between pH 8 and 9. When N-alpha-benzoyl-DL-arginine-p-nitroanilide.HCl (BAPNA) was used as a substrate, the Km and Vmax were 1.17 +/- .05 x 10(-3) M and 1.50 +/- .07 x 10(4) mumol/min.milligram, respectively. Turkey acrosin amidase activity was inhibited by aprotinin, ovomucoid, soybean trypsin inhibitor, benzamidine, p-aminobenzamidine, and zinc.