Abstract
1. It has been shown that the hydrolysis of benzoyl-L-arginine amide by trypsin does not follow the conventional first order kinetics. The constant value of k3 which is independent of both enzyme and sub-strate concentration was obtained from integration of Michaelis-Menten equation.
2. The existence of a group with pK'H=6.28 at 30° and the heat of ionization=7.1 Kcal. mole-1 in trypsin molecule was assumed from the pH dependence on the catalytic activity of trypsin. These values were very close to the figures quoted by Gutfreund.
3. The temperature dependence of the trypsin catalyzed reaction was observed and the heats of enzyme-substrate complex formation and thet of the activation were calculated as 5.9 and 12.3 Kcal. mole-1, respectively.
The authors indebted to Prof. K. Kaziro for his continuous help and stimulating discussion. The authors also express their gratitude to the Ministry of Education for the aid of the Scientific Research Fund.
