PURIFICATION AND PROPERTIES OF OXALATE OXIDASE FROM SORGHUM LEAVES

被引：17

作者：

PUNDIR, CS

机构：

[1] Biochemistry Research Laboratory, Department of Bio-Sciences, Maharshi Dayanand University, Rohtak

来源：

PHYTOCHEMISTRY | 1991年 / 30卷 / 04期

关键词：

SORGHUM-VULGARE; GRAMINEAE; LEAVES; OXALATE OXIDASE; OXALATE; OXALATE OXIDATION; FLAVOPROTEIN; FE2+;

D O I：

10.1016/S0031-9422(00)95173-2

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：

An oxalate oxidase (oxalate: oxygen oxidoreductase EC 1.2.3.4) was purified ca 25-fold from Sorghum leaves. The enzyme has M(r) of ca 62 000 and an optimum pH of 4.3 at 40-degrees. The enzyme activity was inhibited by alpha,alpha'-dipyridyl which could be specifically reversed by Fe2+. The enzyme was unaffected by Na+ in physiological concentration range. FAD strongly stimulated the enzyme. The UV and visible spectra of the enzyme closely corresponded to those of a flavoprotein.

引用

页码：1065 / 1067

页数：3

共 21 条

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