Identification of a thylakoid peroxidase of barley which oxidizes hydroquinone

被引：28

作者：

Zapata, JM ^{[1
]}

Sabater, B ^{[1
]}

Martín, M ^{[1
]}

机构：

[1] Univ Alcala de Henares, Dept Biol Vegetal Fisiol Vegetal, Madrid 28871, Spain

来源：

PHYTOCHEMISTRY | 1998年 / 48卷 / 07期

关键词：

Hordeum vulgare; Gramineae; barley; chloroplasts; peroxidase; photooxidative stress; quinone oxidation; thylakoid;

D O I：

10.1016/S0031-9422(98)00133-2

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：

The oxidation of hydroquinone by two peroxidases (EC 1.11.1.7) fractions obtained from barley leaves has been studied. The results indicated that thylakoid contains hydroquinone peroxidase which may be distinguished from soluble peroxidase by apparent K(M)s, influence of pH on activity and zymographic assays. Appropriate controls indicated that thylakoid peroxidase was not a contamination from other cellular fractions. Thylakoid peroxidase may be solubilized by Triton-containing buffers but not by buffers without detergent and can also be distinguished of other guaiacol peroxidases (as cell wall peroxidase) and of thylakoid ascorbate peroxidase (EC 1.11.1.11) by zymographic assays End stability and kinetic properties. The reduced form of quinone electron carrier of thylakoids may be substrates of HQ peroxidase. (C) 1998 Elsevier Science Ltd. All rights reserved.

引用

页码：1119 / 1123

页数：5

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