| SDS水相胶束体系中酶促反应的热动力学研究 |
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| 引用本文： | 谢修银.SDS水相胶束体系中酶促反应的热动力学研究[J].长江大学学报,2004,1(1):70-73. |
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| 作者姓名： | 谢修银 |
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| 作者单位： | 长江大学化学与环境工程学院,434020 |
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| 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.
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| 关 键 词： | 辣根过氧化物酶(HRP) 邻苯二胺(OPD) 水相胶束 热动力学 |
| 文章编号： | 1009-0010(2004)01-0070-04 |
| 修稿时间： | 2003年9月11日 |
THERMOKINETIC STUDIES ON ENZYME CATALYTIC REACTION IN SDS AQUEOUS MICELLE SYSTEM |
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| Xie Xiuyin.THERMOKINETIC STUDIES ON ENZYME CATALYTIC REACTION IN SDS AQUEOUS MICELLE SYSTEM[J].Journal of Yangtze University,2004,1(1):70-73. |
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| Authors: | Xie Xiuyin |
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| Abstract: | 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. |
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| Keywords: | horseradish peroxidase (HRP) o-phenylenediamine (OPD) aqueous micelle thermokinetics |
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