PURIFICATION AND PARTIAL CHARACTERIZATION OF BEEF-LIVER GLUCONOLACTONASE

被引：16

作者：

BAILEY, GD ^{[1
]}

ROBERTS, BD ^{[1
]}

BUESS, CM ^{[1
]}

CARPER, WR ^{[1
]}

机构：

[1] WICHITA STATE UNIV, DEPT CHEM, WICHITA, KS 67208 USA

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1979年 / 192卷 / 02期

关键词：

D O I：

10.1016/0003-9861(79)90118-8

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：

Gluconolactonase is isolated and purified from beef liver. The molecular weight is estimated at 233,000 and that of its six similar subunits is 39,400. The pH maximum is 7.1 in 50 mm Tris-acetate buffer at 27 °C. Km and Vm values of 9.1 mm and 1.62 mmol/min/ mg, respectively, were obtained at 27 °C in 50 mm Tris-HCl buffer. This enzyme requires a divalent metal for activity, with manganese being preferred over magnesium. A subcellular fractionation study indicates that gluconolactonase is located primarily in the cytosol, and its hepatic concentration is 2.3 μmol/kg of hepatic tissue. © 1979.

引用

页码：482 / 488

页数：7

共 29 条

[1]

BRODIE AF, 1955, J BIOL CHEM, V212, P677

[2] KINETIC STUDY OF PIG LIVER GLUCOSE DEHYDROGENASE [J].