PURIFICATION OF GLUTAMINE-SYNTHETASE FROM AZOTOBACTER AND OTHER PROCARYOTES BY BLUE SEPHAROSE CHROMATOGRAPHY

被引：25

作者：

LEPO, JE ^{[1
]}

STACEY, G ^{[1
]}

WYSS, O ^{[1
]}

TABITA, FR ^{[1
]}

机构：

[1] UNIV TEXAS, DEPT MICROBIOL, AUSTIN, TX 78712 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 568卷 / 02期

基金：

美国国家科学基金会;

关键词：

(Purification); Cibacron Blue-Sepharose; Glutamine synthetase;

D O I：

10.1016/0005-2744(79)90311-5

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：

We report the facile purification of glutamine synthetase (l-glutamate: ammonia ligase (adenosine 5′-diphosphate-forming), EC 6.3.1.2) in both the adenylylated and unadenylylated form, from Azotobacter vinelandii ATCC 12837. A general affinity column, which used as an affinity ligand Reactive blue 2 dye (Cibacron blue) covalently linked to Agarose, was employed as an efficient first step of purification. Further purification to electrophoretic homogeneity employed DEAE-cellulose chromatography and an additional Affigel chromatographic step. The method was used successfully to prepare glutamine synthetase from Escherichia coli, Rhodopseudomonas sphaeroides and Anabaena sp. strain CA. © 1979.

引用

页码：428 / 436

页数：9

共 25 条

[1] DISC ELECTROPHORESIS .2. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS [J].