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黄嘌呤氧化酶催化儿茶酚胺氧化。

Catecholamines oxidation by xanthine oxidase.

作者信息

Foppoli C, Coccia R, Cini C, Rosei M A

机构信息

CNR Center of Molecular Biology, University of Rome, La Sapienza, Italy.

出版信息

Biochim Biophys Acta. 1997 Mar 15;1334(2-3):200-6. doi: 10.1016/s0304-4165(96)00093-1.

Abstract

Dopamine and structurally related catecholamines in the presence of hydrogen peroxide are oxidized in vitro by xanthine oxidase producing the corresponding melanin pigments. The kinetic parameters of the reaction, measured as aminochrome formation, have been calculated. The rate of peroxidation depends on enzyme and hydrogen peroxide concentration. The optimum pH for the peroxidative activity of the enzyme is around 8.5. Activation of the peroxidative reaction is also elicited by catechol compounds through a redox cycle mechanism. Implications about the possible biochemical relevance of xanthine oxidase activity on catecholamines oxidation are discussed.

摘要

多巴胺及结构相关的儿茶酚胺类物质在过氧化氢存在的情况下,可被黄嘌呤氧化酶在体外氧化,生成相应的黑色素。已计算出以氨基色素形成为指标的该反应动力学参数。过氧化速率取决于酶和过氧化氢的浓度。该酶过氧化活性的最适pH约为8.5。儿茶酚化合物也可通过氧化还原循环机制引发过氧化反应的激活。文中讨论了黄嘌呤氧化酶活性对儿茶酚胺氧化可能具有的生化相关性。

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