New affinity resin for purification of cap-binding proteins

被引：0
|
作者：
Jankowska-Anyszka, M
Nogalski, M
Darzynkiewicz, E
机构：
[1] Univ Warsaw, Dept Chem, PL-02093 Warsaw, Poland
[2] Univ Warsaw, Dept Biophys, Inst Expt Phys, PL-02093 Warsaw, Poland
来源：
NUCLEOSIDES NUCLEOTIDES & NUCLEIC ACIDS | 2005年 / 24卷 / 5-7期
关键词：
RECOGNITION;
D O I：
10.1081/NCN-200061782
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：
Cap binding proteins, which recognize the cap structure present at 5' termini of RNA polymerase H transcripts, have been routinely isolated and purified using affinity resins with mononucleotide cap analogs attached. Here we present a new methodology in which dinucleotide cap analog, m(7) GpppG, has been linked to the EAH-Sepharose. The method is based on derivatization of 2, 3'-cis diol of the second nucleotide within the cap structure, with levulinic acid, and subsequent coupling of resulted acetal through its carboxylic group with aminohexyl-agarose.
引用
收藏
页码：503 / 506
页数：4
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