PURIFICATION OF 2 FORMS OF BOVINE LIVER-GLYCOGEN PHOSPHORYLASE-B WITH DISTINCT SUBUNIT COMPOSITION

被引：3

作者：

ARTIGAS, AC ^{[1
]}

BARON, C ^{[1
]}

PARODYMORREALE, A ^{[1
]}

机构：

[1] UNIV GRANADA,FAC CIENCIAS,DEPT QUIM FIS,E-18071 GRANADA,SPAIN

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1994年 / 5卷 / 02期

关键词：

D O I：

10.1006/prep.1994.1025

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The procedures for the purification of two forms of bovine liver glycogen phosphorylase b are described. Both forms showed a single band in nondenaturing gel electrophoresis. Gel electrophoresis in the presence of sodium dodecyl sulfate produced a single-band pattern for one of the enzyme forms (phosphorylase bl) and a triple-band pattern for the other (phosphorylase b3). Molecular weights associated with these bands were 97 kDa in the first case and 97, 55, and 40 kDa in the second. The yield from 1 kg of liver was approximately 10 mg for phosphorylase bl and 140 mg for phosphorylase b3. The specific activity was 40-44 U/mg in both cases. As phosphorylase bl is composed of just one kind of monomer, it is a novel bovine liver phosphorylase b structure. (C) 1994 Academic Press, Inc.

引用

页码：157 / 163

页数：7

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