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微量热法研究酪氨酸酶催化氧化反应
引用本文:龙姝.微量热法研究酪氨酸酶催化氧化反应[J].长沙理工大学学报(自然科学版),2003(Z1).
作者姓名:龙姝
作者单位:长沙电力学院侯家塘校区基础课部 湖南长沙410015
摘    要:在恒温条件下从嗜麦芽假单胞菌中获得酪氨酸酶 ,利用微量热法测定了酪氨酸酶催化氧化酪氨酸反应的动力学性质 ,并得出该反应符合Michaelis -Menten动力学的结论。该方法不需要将酶提纯 ,可以原位测定酶的活性。

关 键 词:微量热法  酪氨酸酶  动力学性质  氧化反应

Studies on the Reaction Tyrosinase-catalyzed Oxidation by Micalorimetry
LONG Shu.Studies on the Reaction Tyrosinase-catalyzed Oxidation by Micalorimetry[J].Journal of Changsha University of Science and Technology:Natural Science,2003(Z1).
Authors:LONG Shu
Abstract:The kinetics properties of the reaction tyrosinase-catalyzed oxidation have been determined by using microcalorimetry at 298.2 K.The tyrosinase is extracted from the Pseudomonas maltophilia.The Michaelis constant of the reaction has determined.The experimental results indicate that the reaction accords with the dynamical mechanism of Michaelis-Menten.Microcalorimetric measurements may be made directly without introducing any chemical and mechanical perturbation into the system.Furthermore,microcalorimetry is a noninvasive and noldestructive manner and allows in situ determine enzyme activity.
Keywords:microcalorimetry  tyrosinase  dynamical mechanism  oxidation
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