Activite trypsique a l'egard de certains substrats chromogenes

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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 Nα 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.