PRODUCTION OF RECOMBINANT AVIDIN IN ESCHERICHIA-COLI

被引：28

作者：

AIRENNE, KJ ^{[1
]}

SARKKINEN, P ^{[1
]}

PUNNONEN, EL ^{[1
]}

KULOMAA, MS ^{[1
]}

机构：

[1] UNIV JYVASKYLA,DEPT BIOL,SF-40100 JYVASKYLA,FINLAND

来源：

GENE | 1994年 / 144卷 / 01期

关键词：

RECOMBINANT DNA; GENE EXPRESSION; CODON CHOICE; PCR AMPLIFICATION; AFFINITY CHROMATOGRAPHY; BIOTIN-BINDING PROTEIN;

D O I：

10.1016/0378-1119(94)90206-2

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

A recombinant avidin (re-Avd), containing amino acids (aa) 1-123 of the native chicken egg-white Avd, was produced in Escherichia coli. When cells were grown at 37 degrees C production was over 1 mu g/ml, due to altering the codon preference of the first ten codons. The re-Avd was recovered as a soluble protein from cells grown at 25 or 30 degrees C, whereas at 37 degrees C it was mostly insoluble in inclusion bodies. Our results indicated that, despite the potentially harmful biotin-binding activity of Avd, it is possible to produce biologically active Avd in E. coli which then can easily be purified by affinity chromatography on a biotin column in a single step.

引用

页码：75 / 80

页数：6

共 25 条

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