GENE SYNTHESIS AND EXPRESSION IN ESCHERICHIA-COLI FOR PUMP, A HUMAN MATRIX METALLOPROTEINASE

被引：31

作者：

YE, QZ ^{[1
]}

JOHNSON, LL ^{[1
]}

BARAGI, V ^{[1
]}

机构：

[1] WARNER LAMBERT PARKE DAVIS,DEPT IMMUNOPATHOL,PARKE DAVIS PHARMACEUT RES DIV,ANN ARBOR,MI 48105

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 186卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)80786-7

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 gene for PUMP (putative metalloproteinase), a human matrix metalloproteinase, was synthesized by a PCR-based method. The DNA fragment of 546 bases containing the PUMP gene was generated by overlap extension of six long oligonucleotides (length ranging from 101 to 116 bases) and subsequent amplification by two short terminal oligonucleotide primers (length from 20 to 48 bases) in one pot without using restriction and ligation enzymes. The synthetic gene was cloned into a T7 expression vector in two ways to express PUMP as a non-fusion protein. Both constructs showed high level expression in E. coli. © 1992 Academic Press, Inc.

引用

页码：143 / 149

页数：7

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