| 双底物酶促反应的热动力学研究 |
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| 引用本文： | 谢修银,李再高.双底物酶促反应的热动力学研究[J].长江大学学报(社会科学版),2003(5). |
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| 作者姓名： | 谢修银 李再高 |
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| 作者单位： | 荆州师范学院化学系 434020
(谢修银)，荆州师范学院化学系 434020(李再高) |
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| 基金项目： | 湖北省教育厅重点项目(2003A0009) |
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| 摘 要： | 利用微量热方法研究了辣根过氧化物酶(HRP)催化H_2O_2氧化邻苯二胺(OPD)的反应。在298.15K,50mM,pH=7.4的磷酸盐缓冲体系中反应消耗1mol H_2O_2的焓变为227.99kJmol~(-1),而消耗1mol OPD的焓变为439.21kJmol~(-1),HRP对底物H_2O_2的米氏常数K_m(H_2O_2)=2.92mM,对底物OPD的米氏常数K_m(OPD)=0.51mM。
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| 关 键 词： | 辣根过氧化物酶(HRP) 邻苯二胺(OPD) 热动力学 双底物酶促反应 |
THERMOKINETIC STUDIES ON DOUBLE SUBSTRATES ENZYME CATALYTIC REACTION |
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| Xie Xiuyin Li Zaigao.THERMOKINETIC STUDIES ON DOUBLE SUBSTRATES ENZYME CATALYTIC REACTION[J].Journal of Yangtze University:Social Sciences,2003(5). |
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| Authors: | Xie Xiuyin Li Zaigao |
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| Abstract: | A double substrates enzyme reaction, which horseradish peroxidase (HRP) catalytic oxide of o -phenylenediamine (OPD) by H2O2, were studied by thermokinetic method. At 298.15K, the total molar enthalpies of the reaction are determined to be 227. 99kjmol -1 and 439.21 kjmol -1 respectively when the reaction use up 1 mol H2O2 or 1 mol OPD in 50 mM, pH =7.4 phosphate salt buffer. The Michaelis constants of the reaction are 2.97 mM to H2O2 and 0.51 mM to OPD. |
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| Keywords: | horseradish peroxidase (HRP) O - phenylenediamine (OPD) thermokinetics double substrates enzymatic reaction |
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