高等学校化学学报 ›› 1991, Vol. 12 ›› Issue (6): 822.

• 论文 • 上一篇    下一篇

酶促反应热动力学方程的研究

梅付名1, 吴鼎泉1, 屈松生1, 杜予民2, 詹东风2   

  1. 1. 武汉大学化学系, 武汉, 430072;
    2. 武汉大学资源研究所
  • 收稿日期:1990-03-07 出版日期:1991-06-24 发布日期:1991-06-24
  • 通讯作者: 吴鼎泉

Studies on Thermokinetic Equation of Enzyme-Catalytic Reaction

Mei Fu-ming1, Wu Ding-quan1, Qu Song-sheng1, Du Yu-min2, Zhan Dong-feng2   

  1. 1. Depart. of Chem., Wuhan Univ., Wuhan, 430072;
    2. Institute of Resource Chemstry, Wuhan University
  • Received:1990-03-07 Online:1991-06-24 Published:1991-06-24

摘要: 由酶促反应速率方程积分式和酶促反应中能量变化与物质参与反应量的关系推出了单底物酶促反应的热动力学方程。并用精氨酸的酶促水解反应进行了验证,求出的米氏常数Km和最大速率Vmax与文献值相符。

关键词: 热动力学方程, 米氏常数, 微量热法

Abstract: The thermokinetie equation in the enzyme-catalytic reaction of the single substrate is suggested from the integral of the rate equation and the relationship between the variation of energy and the amount of reactants in the reaction and is tested with the hydrolysis reaction between arginine and arginase. The calculated values of the Michaelis constant Km and the maximum rate Vmax are 4.98×10-3mol/Land 2.33×10-5 mol/L·s, respectively, in agreement with those in the literature.

Key words: Thermokinetic equation, Michaelis constant, Microcalorimetric method

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