Kinetics of Inactivation of Aminoacylase I During Modification of Its Thiol Groups by DPDS and PCMB  

作　　者：王洪睿 阴勇 张英侠 王希成 周海梦 

机构地区：[1]Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, PRC [2]National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing 100080, PRC)

出　　处：《Science China Chemistry》1993年第1期52-59,共8页中国科学（化学英文版）

摘　　要：The kinetics theory of the substrate reaction during modification of enzyme activity previously described by Tsou has been applied to a study on the kinetics of the course of inactivation of aminoacylase I by DPDS and PCMB.From the results obtained we have found that the inactivation reaction of aminoacylase I by DPDS is noncomplexing inhibition,and PCMB reaction is complexing inhibition.The microscopic constants for the reaction of the inactivator with free enzyme and the enzyme-substrate complex were determined.The kinetics theory of the substrate reaction during modification of enzyme activity previously described by Tsou has been applied to a study on the kinetics of the course of inactivation of aminoacylase I by DPDS and PCMB.From the results obtained we have found that the inactivation reaction of aminoacylase I by DPDS is noncomplexing inhibition,and PCMB reaction is complexing inhibition.The microscopic constants for the reaction of the inactivator with free enzyme and the enzyme-substrate complex were determined.

关 键 词：AMINOACYLASE CHEMICAL MODIFICATION INHIBITION kinetics. 

分 类 号：O6[理学—化学]