LIPOXYGENASE-CATALYZED OXIDATION OF CATECHOLAMINES

被引：70

作者：

ROSEI, MA ^{[1
]}

BLARZINO, C ^{[1
]}

FOPPOLI, C ^{[1
]}

MOSCA, L ^{[1
]}

COCCIA, R ^{[1
]}

机构：

[1] CNR, CTR MOLEC BIOL, ROME, ITALY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 200卷 / 01期

关键词：

D O I：

10.1006/bbrc.1994.1454

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Dopa and structurally related catecholamines in presence of hydrogen peroxide are oxidized in vitro by soybean lipoxygenase producing the corresponding melanin pigments. The kinetic parameters of the catecholasic reaction, measured as aminochrome formation, have been calculated. The rate of peroxidation depends on catecholamine and hydrogen peroxide concentration. The optimum: pH for the peroxidative activity of the enzyme is around 8.5. The enzyme, at higher pH values (pH 9 - 9.5), is also able to perform an oxidative reaction of the substrates. Implications of the possible biochemical relevance of the reactions are discussed. (C) 1994 Academic Press, Inc.

引用

页码：344 / 350

页数：7

共 21 条

[1] INACTIVATION OF PEROXIDASE BY HYDROGEN-PEROXIDE AND ITS PROTECTION BY A REDUCTANT AGENT [J].