Inhibition of rat liver and kidney arginase by cadmium ion

被引：13

作者：

Tormanen, CD ^{[1
]}

机构：

[1] Cent Michigan Univ, Dept Chem, Mt Pleasant, MI 48859 USA

来源：

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY | 2006年 / 21卷 / 01期

关键词：

arginase; cadmium; inhibition; rat liver; rat kidney;

D O I：

10.1080/14756360500483420

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：

Cadmium ion activates arginase from many species of organisms but is an inhibitor of arginase from many other species. The purpose of this study was to investigate the inhibition of rat liver and kidney arginase by cadmium ion. Rat kidney arginase was inhibited by much lower concentrations of cadmium ion than rat liver arginase. Cadmium ion was a mixed noncompetitive inhibitor of both rat liver and kidney arginase. Cadmium ion enhanced the substrate activation of rat kidney arginase while still inhibiting the enzyme. Cadmium ion prevented the substrate inhibition of rat kidney arginase by fluoride while still inhibiting the enzyme. Cadmium ion also inhibited rat kidney arginase in the presence of manganese ion.

引用

页码：119 / 123

页数：5

共 37 条

[1] Comparison of the inhibitory effects of mercury and cadmium on the creatine kinase from Electrophorus electricus (L) [J].

Araujo, GMN ;

Silva, CB ;

HassonVoloch, A .

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 1996, 28 (04) :491-497

[2] Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers [J].

Axelrod, HL ;

Abresch, EC ;

Paddock, ML ;

Okamura, MY ;

Feher, G .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (04) :1542-1547

[3] Cadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complex [J].

Banerjee, S ;

Flores-Rozas, H .

NUCLEIC ACIDS RESEARCH, 2005, 33 (04) :1410-1419

[4] Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily [J].

Bewley, MC ;

Jeffrey, PD ;

Patchett, ML ;

Kanyo, ZF ;

Baker, EN .

STRUCTURE WITH FOLDING & DESIGN, 1999, 7 (04) :435-448

[5] Inhibitor coordination interactions in the binuclear manganese cluster of arginase [J].

Cama, E ;

Pethe, S ;

Boucher, JL ;

Han, SF ;

Emig, FA ;

Ash, DE ;

Viola, RE ;

Mansuy, D ;

Christianson, DW .

BIOCHEMISTRY, 2004, 43 (28) :8987-8999

[6] A COMPARATIVE STUDY OF MOLLUSCAN AND MAMMALIAN ARGINASES [J].

CAMPBELL, JW .

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY, 1966, 18 (01) :179-&

[7] PROPERTIES OF AMPHIBIAN RENAL ARGINASE .2. IONIC STIMULATION AND OTHER PROPERTIES OF MICROSOMAL FRACTION [J].

CARLISKY, NJ .

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY, 1972, 42 (1B) :73-&

[8] PROPERTIES OF ARGINASE FROM THE FOOT MUSCLE OF CHITON-LATUS [J].

CARVAJAL, N ;

KESSI, E ;

BIDART, J ;

ROJAS, A .

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 1988, 90 (02) :385-388

[9] PROPERTIES OF ARGINASE FROM THE SEA MOLLUSK CONCHOLEPAS-CONCHOLEPAS [J].

CARVAJAL, N ;

BUSTAMANTE, M ;

HINRICHSEN, P ;

TORRES, A .

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 1984, 78 (03) :591-594

[10] SUBCELLULAR-LOCALIZATION, METAL-ION REQUIREMENT AND KINETIC-PROPERTIES OF ARGINASE FROM THE GILL TISSUE OF THE BIVALVE SEMELE SOLIDA [J].

CARVAJAL, N ;

URIBE, E ;

TORRES, C .

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 1994, 109 (04) :683-689

← 1 2 3 4 →