INTERACTION OF ARGINASE WITH METAL-IONS - STUDIES OF THE ENZYME FROM HUMAN LIVER AND COMPARISON WITH OTHER ARGINASES

被引:47
作者
CARVAJAL, N
TORRES, C
URIBE, E
SALAS, M
机构
[1] Departamento de Biologia Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1995年 / 112卷 / 01期
关键词
MN2+; METAL IONS; HEAT INACTIVATION; TRYPSIN INACTIVATION; TRYPTOPHAN FLUORESCENCE; KINETICS; HUMAN LIVER; ARGINASE;
D O I
10.1016/0305-0491(95)00027-6
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
As determined by atomic absorption, fully activated human liver arginase contained 1.1 +/- 0.1 Mn2+/subunit. Upon dissociation to inactive subunits (<0.01 Mn2+/subunit), there was decreased intensity and a red shift in the tryptophan fluorescence emission spectra of the enzyme, and the resulting species were markedly sensitive to thermal and proteolytic inactivation by trypsin. Arginine and lysine specifically protected the subunits from heat inactivation, Subunit activation by Mn2+ followed hyperbolic kinetics (K-d = 0.08 +/- 0.01 mu M). In addition to Mn2+, Ni2+ and Co2+ converted inactive subunits into active monomers, and favoured their association to the oligomeric state of the enzyme (M(r) = 120,000 +/- 2000). The replacement of Mn2+ by Ni2+ or Co2+ resulted in significant changes in V-max without any change in the K-m values for the substrates (arginine or canavanine) or the K-i value for lysine inhibition, The results support our previous suggestion (Carvajal ed al., 1994) that Mn2+ is not essential for substrate binding to arginase, and substantiates the conclusion that species differences may exist in the interaction of arginase with metal ions.
引用
收藏
页码:153 / 159
页数:7
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