Immunoaffinity purification of the human multisubunit transcription factor IIH

被引：25

作者：

LeRoy, G ^{[1
]}

Drapkin, R ^{[1
]}

Weis, L ^{[1
]}

Reinberg, D ^{[1
]}

机构：

[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Howard Hughes Med Inst, Div Nucl Acid Enzymol,Dept Biochem, Piscataway, NJ 08854 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1998年 / 273卷 / 12期

关键词：

D O I：

10.1074/jbc.273.12.7134

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：

A procedure to immunoaffinity purify the human transcription factor IIH (TFIIH) was developed using a monoclonal antibody that recognizes an epitope in ERCC3 (XPB), the largest subunit of TFIIH. The epitope recognized by the monoclonal antibody was mapped to 20 amino acids. A peptide containing the epitope was capable of displacing TFIIH from an immunoaffinity column containing the monoclonal antibody. The immunoaffinity purification procedure described allows a simple and efficient method to purify both the "core" and "holo" TFIIH complexes.

引用

页码：7134 / 7140

页数：7

共 55 条

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