LeRoy G, Drapkin R, Weis L, Reinberg D
Howard Hughes Medical Institute, Division of Nucleic Acid Enzymology, Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854-5635, USA.
J Biol Chem. 1998 Mar 20;273(12):7134-40. doi: 10.1074/jbc.273.12.7134.
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.
利用一种单克隆抗体开发了一种免疫亲和纯化人转录因子IIH（TFIIH）的方法，该单克隆抗体可识别TFIIH最大亚基ERCC3（XPB）中的一个表位。单克隆抗体识别的表位被定位到20个氨基酸。含有该表位的肽能够从含有单克隆抗体的免疫亲和柱上置换TFIIH。所述的免疫亲和纯化方法提供了一种简单有效的方法来纯化“核心”和“全酶”TFIIH复合物。
