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过氧化物酶催化硫醇的过氧化物酶-氧化酶氧化的能力。

Abilities of peroxidases to catalyse peroxidase-oxidase oxidation of thiols.

作者信息

Svensson B E

机构信息

Research and Development Laboratories, Astra Alab AB, Södertälje, Sweden.

出版信息

Biochem J. 1988 Dec 15;256(3):757-62. doi: 10.1042/bj2560757.

Abstract

The abilities of various peroxidases to catalyse the peroxidase-oxidase oxidation of seven aminothiols were studied. Cysteamine and cysteine esters were found to be peroxidase-oxidase substrates for eosinophil peroxidase and myeloperoxidase, whereas other thiols tested were inactive or poorly active with these peroxidases. With lactoperoxidase and horseradish peroxidase, all the tested thiols were inactive or poorly active as peroxidase-oxidase substrates. These studies suggest that a main reason for thiols being poor peroxidase-oxidase substrates is because these thiols are poor peroxidatic substrates.

摘要

研究了各种过氧化物酶催化七种氨基硫醇的过氧化物酶-氧化酶氧化反应的能力。发现半胱胺和半胱氨酸酯是嗜酸性粒细胞过氧化物酶和髓过氧化物酶的过氧化物酶-氧化酶底物,而测试的其他硫醇对这些过氧化物酶无活性或活性较差。对于乳过氧化物酶和辣根过氧化物酶,所有测试的硫醇作为过氧化物酶-氧化酶底物均无活性或活性较差。这些研究表明,硫醇作为过氧化物酶-氧化酶底物活性较差的主要原因是这些硫醇是较差的过氧化物底物。

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Thiols as peroxidase substrates.硫醇作为过氧化物酶底物。
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The oxidation of dithiothreitol by peroxidases and oxygen.过氧化物酶和氧气对二硫苏糖醇的氧化作用。
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