Purification of histone deacetylase HD1‐A of germinating maize embryos

FEBS Letters

Goralik-Schramel, Maria¹  Brosch, Gerald¹  Loidl, Peter¹ 

[1] Department of Microbiology, University of Innsbruck, Medical School, A-6020 Innsbruck, Austria

关键词: Chromatin;    Histone acetylation;    Histone deacetylase;    Nucleosome;    Nuclear protein;    Maize;   

DOI  :  10.1016/0014-5793(96)00909-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 77 000-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 were 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.

【 授权许可】

Unknown