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Kinetic characterization of dopamine as a suicide substrate of tyrosinase.

作者信息

Tudela J, Garcia-Canovas F, Varón R, Jimenez M, Garcia-Carmona F, Lozano J A

机构信息

Departmento de Bioquimica, Facultad de Medicina, Universidad de Murcia, Spain.

出版信息

J Enzyme Inhib. 1987;2(1):47-56. doi: 10.3109/14756368709030356.

DOI:10.3109/14756368709030356
PMID:3149665
Abstract

A kinetic study of the inactivation of frog epidermis tyrosinase by a suicide substrate dopamine hydrochloride is described. The kinetic parameters and constants which characterize this reaction have been determined and the effects of pH and the stoichiometric inhibition by chloride have been considered.

摘要

相似文献

1
Kinetic characterization of dopamine as a suicide substrate of tyrosinase.
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Experimental approach to the kinetic study of unstable site-directed irreversible inhibitors: kinetic origin of the apparent positive co-operativity arising from inactivation of trypsin by p-amidinophenylmethanesulphonyl fluoride.不稳定的定点不可逆抑制剂动力学研究的实验方法:对氨基苯甲脒基甲磺酰氟使胰蛋白酶失活产生的表观正协同性的动力学起源
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A kinetic study of the suicide inactivation of an enzyme measured through coupling reactions. Application to the suicide inactivation of tyrosinase.
通过偶联反应测定酶自杀失活的动力学研究。酪氨酸酶自杀失活的应用。
Biochem J. 1989 Sep 1;262(2):597-603. doi: 10.1042/bj2620597.
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A kinetic study of irreversible enzyme inhibition by an inhibitor that is rendered unstable by enzymic catalysis. The inhibition of polyphenol oxidase by L-cysteine.一项关于酶催化作用下会变得不稳定的抑制剂对不可逆酶抑制作用的动力学研究。L-半胱氨酸对多酚氧化酶的抑制作用。
Biochem J. 1991 Aug 1;277 ( Pt 3)(Pt 3):869-74. doi: 10.1042/bj2770869.