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Thermokinetic Study on the Reversible Competitive Inhibition of Bovine Liver Arginase
引用本文:谢修银,汪存信,王志勇. Thermokinetic Study on the Reversible Competitive Inhibition of Bovine Liver Arginase[J]. 中国化学, 2004, 22(11): 1257-1261. DOI: 10.1002/cjoc.20040221109
作者姓名:谢修银  汪存信  王志勇
作者单位:College of Chemistry and Environment Engineering,Yangtze University,College of Chemistry and Molecular Science,Wuhan University,Wuhan,Hubei 430072,China,College of Chemistry and Molecular Science,Wuhan University,Wuhan,Hubei 430072,China Jingzhou,Hubei 434104,China,College of Chemistry and Molecular Science,Wuhan University,Wuhan,Hubei 430072,China
基金项目:Project supported by the National Natural Science Foundation of China (No. 30070200) and the Major Project of Hubei Province,Department of Education,China (No. 2003A009).
摘    要:Introduction Arginase (EC 3.5.3.1) is a widespread and very im-portant enzyme in mammals, which specifically cata-lyzes the hydrolysis of L-arginine to urea and the non-protein amino acid L-ornithine, a key step in the urea cycle.1 Urea is the principal metabolite for disposal of nitrogen as a neutral and nontoxic waste product formed during amino acid metabolism in mammals. L-ornithine serves as a biosynthetic precursor to L-proline and the polyamines such as putrescine, sper-mine (in eucar…

关 键 词:热力学 牛 肝脏 精氨酸酶 可逆竞争抑制 L-精氨酸 L-赖氨酸

Thermokinetic Study on the Reversible Competitive Inhibition of Bovine Liver Arginase
XIE,Xiu-Yin,a,bWANG,Cun-Xinb WANG,Zhi-Yongb a College of Chemistry and Environment Engineering,Yangtze University,Jingzhou,Hubei ,China b College of Chemistry and Molecular Science,Wuhan University,Wuhan,Hubei ,China. Thermokinetic Study on the Reversible Competitive Inhibition of Bovine Liver Arginase[J]. Chinese Journal of Chemistry, 2004, 22(11): 1257-1261. DOI: 10.1002/cjoc.20040221109
Authors:XIE  Xiu-Yin  a  bWANG  Cun-Xinb WANG  Zhi-Yongb a College of Chemistry  Environment Engineering  Yangtze University  Jingzhou  Hubei   China b College of Chemistry  Molecular Science  Wuhan University  Wuhan  Hubei   China
Affiliation:XIE,Xiu-Yin*,a,bWANG,Cun-Xinb WANG,Zhi-Yongb a College of Chemistry and Environment Engineering,Yangtze University,Jingzhou,Hubei 434104,China b College of Chemistry and Molecular Science,Wuhan University,Wuhan,Hubei 430072,China
Abstract:A new thermokinetic reduced extent method for studying of the reversible Competitive inhibition of single substrate enzyme‐catalyzed reactions was proposed in this paper. The reaction that arginase‐catalyzed hydrolysis of L‐arginine to L‐ornithine and urea and the inhibition of this reaction by the product, L‐ornithine, and exogenous L‐lysine were studied at 37 °C in 40 mmol?L?1 sodium barbiturate‐HC1 buffer solution (pH=9.4). Michealis constant Km for arginine and maximum velocity Vm of the reaction were determined to be 5.14 mmol.L?1 and 1.13X 10?2 mmol‐L?1.s‐1, respectively. The product inhibition constant Kp and inhibitory constant K1 of L‐lysine were determined to be 1.18 and 5.6 mmol.L?1, respectively. All the results have better repeatability and self‐consistency and are in agreement with literature values. This new method using more direct thermal information from the process would give more reliable kinetic information than the traditional initial rate method.
Keywords:bovine liver arginase   reversible competitive inhibition   L-arginine   L-lysine   thermokinetics
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