HYDROPEROXIDE ANION, HO2-, IS AN AFFINITY REAGENT FOR THE INACTIVATION OF YEAST CU,ZN SUPEROXIDE-DISMUTASE - MODIFICATION OF ONE HISTIDINE PER SUBUNIT

被引：102

作者：

BLECH, DM ^{[1
]}

BORDERS, CL ^{[1
]}

机构：

[1] COLL WOOSTER, DEPT CHEM, WOOSTER, OH 44691 USA

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1983年 / 224卷 / 02期

关键词：

D O I：

10.1016/0003-9861(83)90245-X

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：

引用

页码：579 / 586

页数：8

共 33 条

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[5] PROPERTIES OF THE CUPRIC SITES IN BOVINE SUPEROXIDE-DISMUTASE STUDIED BY NUCLEAR-MAGNETIC-RELAXATION MEASUREMENTS
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[7] IDENTIFICATION OF ARG-143 AS THE ESSENTIAL ARGINYL RESIDUE IN YEAST CU,ZN SUPEROXIDE-DISMUTASE BY USE OF A CHROMOPHORIC ARGININE REAGENT
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[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1980, 96 (03) : 1071 - 1078
[8] BORDERS CL, 1982, FED PROC, V41, P1173
[9] REDUCTION AND INACTIVATION OF SUPEROXIDE-DISMUTASE BY HYDROGEN-PEROXIDE
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[J]. BIOCHEMICAL JOURNAL, 1974, 139 (01) : 43 - 48
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