Research note: kinetic and inhibition studies with turkey acrosin.
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.
Richardson
M E
ME
Department of Animal, Dairy, and Veterinary Sciences, Clemson University, South Carolina 29634.
Korn
N
N
Bodine
A B
AB
Thurston
R J
RJ
D000176:Acrosin / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000581:Amidohydrolases / Q000378:metabolism; D000818:Animals; D001586:Benzoylarginine Nitroanilide / Q000378:metabolism; D004950:Esterases / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008297:Male; D013094:Spermatozoa / Q000201:enzymology*; D014422:Turkeys
D001586:Benzoylarginine Nitroanilide; D004950:Esterases; D000176:Acrosin; D000581:Amidohydrolases