SDS水相胶束体系中酶促反应的热动力学研究  

THERMOKINETIC STUDIES ON ENZYMECATALYTIC REACTION IN SDS AQUEOUS MICELLE SYSTEM

作　　者：谢修银[1] 

机构地区：[1]长江大学化学与环境工程学院,434020

出　　处：《长江大学学报（自然科学版）》2004年第1期70-73,共4页Journal of Yangtze University(Natural Science Edition)

基　　金：湖北省教育厅重点项目(2003A009)

摘　　要：　在298.15K十二烷基硫酸钠(SDS)的水相胶束体系中,利用微量热方法研究了辣根过氧化物酶(HRP)催化H2O2氧化邻苯二胺(OPD)的反应.SDS作为一种蛋白质变性剂,不仅能够使HRP变性失去部分活性,而且还能使HRP对底物OPD的米氏常数Km(OPD)和最大反应速率都比其在缓冲体系中小;而在SDS溶胶中,OPD相对过量时,HRP对底物H2O2不符合米氏机理.A double substrates enzyme reaction, the horseradish peroxidase (HRP) catalytic oxide of o-phenylenediamine (OPD) by H_2O_2, was studied by thermokinetic method at 298.15K in a SDS aqueous micelle system. As a denaturant for protein, SDS not only makes the HRP lose its activity because of denaturalization, but also decrease the Michaelis constant and the maximum velocity of the reaction for the substrate OPD. When OPD is relatively excessive in the reaction system, SDS makes the reaction unfit the Michaelis mechanism for substrate H_2O_2.

关 键 词：胶束体系 SDS 动力学研究 酶促反应 水相 十二烷基硫酸钠 辣根过氧化物酶 H2O2 HRP 邻苯二胺 缓冲体系 反应速率 米氏常数 15K 变性剂 蛋白质 微量热 底物 

分 类 号：Q55[生物学—生物化学] O614.31[理学—无机化学]