Abstract
Tryptic hydrolysis of different arginine nitroanilides was studied. Para-nitroanilide is the most readily hydrolyzed substrate, ortho derivative is 5 times less sensitive and meta derivative is a very weak substrate. When the benzoyl group bound on the N α arginine of BAPNA is replaced by a carbobenzoxy group (L-ZAPNA), the tryptic hydrolysis is increased by a factor of 3. With this latter substrate, the kinetic constants are determined for two forms, native and Nϵ-acetylated of porcine and bovine trypsin. Evidence is presented that the rate of hydrolysis is both related to the global and local charges of the enzyme.
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