CARBOXYLESTERASES (EC 3.1.1) . MOLECULAR WEIGHT AND EQUIVALENT WEIGHT OF PIG LIVER CARBOXYLESTERASE

被引：55

作者：

HORGAN, DJ

DUNSTONE, JR

STOOPS, JK

WEBB, EC

ZERNER, B

机构：

[1] Department of Biochemistry, University of Queensland, St. Lucia

[2] Department of Physical Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra, A. C. T

来源：

BIOCHEMISTRY | 1969年 / 8卷 / 05期

关键词：

D O I：

10.1021/bi00833a034

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：

The molecular weight of pig liver carboxylesterase (~88% pure) has been determined as 163,000 (±15,000). The enzyme has two active sites per molecular weight of 163,000 as shown by titration with pnitrophenyl dimethylcarbamate and p-nitrophenyl diethyl phosphate. The enzyme undergoes slow irreversible inactivation at pH 5, but on dilution at pH 7.5, the enzyme dissociates apparently into half-molecules which are active. No evidence has been obtained for the dissociation of the enzyme into species of mol wt ~40,000, either at pH 8 or in 8 M urea. © 1969, American Chemical Society. All rights reserved.

引用

页码：2006 / &

共 41 条

[1]

ADLER AJ, 1961, J BIOL CHEM, V236, P3240

[2] GEL-FILTRATION BEHAVIOUR OF PROTEINS RELATED TO THEIR MOLECULAR WEIGHTS OVER A WIDE RANGE [J].