THE INTERACTION OF MEMBRANE DNA-BINDING PROTEIN WITH DNA

被引：0

作者：

GABRIELYAN, AG

ARAKHELYAN, HH

ZAKHARYAN, RA

机构：

来源：

JOURNAL OF MOLECULAR STRUCTURE-THEOCHEM | 1994年 / 117卷

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D O I：

暂无

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

A 31-kDa protein specifically binding to double-stranded DNA (ds-DNA) was isolated from plasmatic membranes of rat liver cells by means of affinity chromatography and high performance liquid chromatography (HPLC). Some of the properties of this protein were determined. Judging by the UV and circular dichroism spectroscopic data, the protein forms a complex with DNA, stabilizing its native structure, mainly in the regions rich in AT pairs. The 31-kDa protein-pAO3 plasmid DNA binding constant was determined by nitrocellulose filter analysis of protein labelled DNA complexes. The results obtained correspond to cooperative binding with DNA molecules of extended interacting ligands, having AT specificity. A possible role of the 31-kDa protein in DNA transmembrane transition processes is discussed.

引用

页码：353 / 358

页数：6

共 26 条

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