PURIFICATION OF ACV SYNTHETASE FROM STREPTOMYCES-CLAVULIGERUS

被引：22

作者：

ZHANG, JY ^{[1
]}

DEMAIN, AL ^{[1
]}

机构：

[1] MIT,DEPT BIOL,CAMBRIDGE,MA 02139

来源：

BIOTECHNOLOGY LETTERS | 1990年 / 12卷 / 09期

关键词：

D O I：

10.1007/BF01088188

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

By a combination of protamine sulfate treatment, ammonium sulfate fractionation, gel filtration and hydrophobic interaction chromatography, an active δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (ACV) synthetase from the prokaryote Streptomyces clavuligerus was purified 135-fold to give a single major protein band on SDS-PAGE. Its size appears to be approximately 360 kDa which is very similar to that of the enzyme from the eukaryote, Cephalosporium acremonium. © 1990 Kluwer Academic Publishers.

引用

页码：649 / 654

页数：6

共 12 条

[1] CELL-FREE SYNTHESIS OF DELTA-(L-ALPHA-AMINOADIPYL)-L-CYSTEINE, THE 1ST INTERMEDIATE OF PENICILLIN AND CEPHALOSPORIN BIOSYNTHESIS [J].