BACULOVIRUS-MEDIATED HIGH-LEVEL EXPRESSION OF A MAMMALIAN DNA METHYLTRANSFERASE

被引：12

作者：

GLICKMAN, JF

REICH, NO

机构：

[1] UNIV CALIF SANTA BARBARA,DEPT CHEM,SANTA BARBARA,CA 93106

[2] UNIV CALIF SANTA BARBARA,PROGRAM BIOCHEM & MOLEC BIOL,SANTA BARBARA,CA 93106

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 204卷 / 03期

关键词：

D O I：

10.1006/bbrc.1994.2562

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：

The murine C-5 cytosine DNA methyltransferase (MTase, E.C.2.1.1.37) containing a hexahistidine affinity leader peptide has been expressed at levels which are at least 50-fold higher than previously reported. The recombinant enzyme has activity levels similar to the wild-type enzyme. The recombinant polypeptide binds to and elutes from a nickel affinity resin (IMAC resin). No dramatic differences in post-translational modification between the wild-type and recombinant enzyme were observed. The recombinant system will be useful in performing site-directed mutagenesis and will facilitate enzymological and biological investigations of this enzyme. (C) 1994 Academic Press, Inc.

引用

页码：1003 / 1008

页数：6

共 16 条

[1] CLONING AND SEQUENCING OF A CDNA-ENCODING DNA METHYLTRANSFERASE OF MOUSE CELLS - THE CARBOXYL-TERMINAL DOMAIN OF THE MAMMALIAN ENZYMES IS RELATED TO BACTERIAL RESTRICTION METHYLTRANSFERASES [J].