BINDING OF COPPER IONS TO COPPER-FREE BOVINE SUPEROXIDE-DISMUTASE - PROPERTIES OF PROTEIN RECOMBINED WITH INCREASING AMOUNTS OF COPPER IONS

被引：27

作者：

RIGO, A

TERENZI, M

VIGLINO, P

CALABRESE, L

COCCO, D

ROTILIO, G

机构：

[1] UNIV VENICE,INST PHYS CHEM,VENICE,ITALY

[2] UNIV CAMERINO,DEPT BIOL CHEM,I-62032 CAMERINO,ITALY

[3] UNIV ROME,DEPT BIOL CHEM,I-00100 ROME,ITALY

[4] UNIV CALABRIA,DEPT CHEM,ARCAVACATA,ITALY

[5] UNIV ROME,CNR,CTR MOLEC BIOL,I-00100 ROME,ITALY

来源：

BIOCHEMICAL JOURNAL | 1977年 / 161卷 / 01期

关键词：

D O I：

10.1042/bj1610031

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：31 / 35

页数：5

共 6 条

[1] STUDIES ON RECONSTITUTION OF BOVINE ERYTHROCYTE SUPEROXIDE DISMUTASE .1. PRESENCE OF FOUR DIVALENT METAL-BINDING SITES ON APO PROTEIN WHICH ARE DIFFERENT FROM NATIVE SITES [J].

FEE, JA .

BIOCHIMICA ET BIOPHYSICA ACTA, 1973, 295 (01) :87-95

[2] MECHANISM OF ACTION OF SUPEROXIDE-DISMUTASE FROM PULSE-RADIOLYSIS AND ELECTRON-PARAMAGNETIC RESONANCE - EVIDENCE THAT ONLY HALF ACTIVE-SITES FUNCTION IN CATALYSIS [J].

FIELDEN, EM ;

ROBERTS, PB ;

BRAY, RC ;

LOWE, DJ ;

MAUTNER, GN ;

ROTILIO, G ;

CALABRESE, L .

BIOCHEMICAL JOURNAL, 1974, 139 (01) :49-60

[3] ENZYME-ACTIVITY OF SUPEROXIDE-DISMUTASE PROTOMERS [J].

MARMOCCHI, F ;

VENARDI, G ;

CAULINI, G ;

ROTILIO, G .

FEBS LETTERS, 1974, 44 (03) :337-339

[4] POLAROGRAPHIC-DETERMINATION OF SUPEROXIDE-DISMUTASE [J].

RIGO, A ;

VIGLINO, P ;

ROTILIO, G .

ANALYTICAL BIOCHEMISTRY, 1975, 68 (01) :1-8

[5] BINDING OF COPPER IONS TO COPPER-FREE BOVINE SUPEROXIDE-DISMUTASE - COPPER DISTRIBUTION IN PROTEIN SAMPLES RECOMBINED WITH LESS THAN STOICHIOMETRIC COPPER ION-PROTEIN RATIOS [J].

RIGO, A ;

VIGLINO, P ;

CALABRESE, L ;

COCCO, D ;

ROTILIO, G .

BIOCHEMICAL JOURNAL, 1977, 161 (01) :27-&

[6] PROPERTIES OF APOPROTEIN AND ROLE OF COPPER AND ZINC IN PROTEIN CONFORMATION AND ENZYME-ACTIVITY OF BOVINE SUPEROXIDE DISMUTASE [J].

ROTILIO, G ;

BOSSA, F ;

AGRO, AF ;

CALABRESE, L ;

BARRA, D ;

MONDOVI, B .

BIOCHEMISTRY, 1972, 11 (11) :2182-+

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