Purification of histone deacetylase HD1-A of germinating maize embryos

被引：27

作者：

Brosch, G

GoralikSchramel, M

Loidl, P

机构：

[1] Department of Microbiology, University of Innsbruck, Medical School

来源：

FEBS LETTERS | 1996年 / 393卷 / 2-3期

关键词：

chromatin; histone acetylation; histone deacetylase; nucleosome; nuclear protein; maize;

D O I：

10.1016/0014-5793(96)00909-X

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：

We have purified the soluble nuclear histone deacetylase HD1-A of germinating maize embryos, By a combination of 6 chromatographic steps we achieved a 77000-fold purification of an enzymatically active protein. Gel filtration chromatography revealed a molecular weight of 45 kDa of the native enzyme and electrophoretic analysis of the purified enzyme by SDS-PAGE resulted in a single band at a molecular weight of 48 kDa, indicating that the enzyme is a monomer protein. When fractions with enzyme activity of different stages of chromatographic purification mere subjected to isoelectric focusing, enzyme activity focused at a pH of around 6.4 as measured in an activity gel assay; second dimension SDS-PAGE again revealed a protein spot at a molecular weight of 48 kDa.

引用

页码：287 / 291

页数：5

共 46 条

[1] A NOVEL YEAST HISTONE DEACETYLASE - PARTIAL CHARACTERIZATION AND DEVELOPMENT OF AN ACTIVITY ASSAY [J].