PURIFICATION AND PARTIAL CHARACTERIZATION OF DELTA-(L-ALPHA-AMINOADIPYL)-L-CYSTEINYL-D-VALINE SYNTHETASE FROM STREPTOMYCES-CLAVULIGERUS

被引：34
作者：
JENSEN, SE
WONG, A
ROLLINS, MJ
WESTLAKE, DWS
机构：
[1] Department of Microbiology, University of Alberta, Edmonton
来源：
JOURNAL OF BACTERIOLOGY | 1990年 / 172卷 / 12期
关键词：
D O I：
10.1128/jb.172.12.7269-7271.1990
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
δ-(L-α-Aminoadipyl)-L-cysteinyl-D-valine synthetase (ACVS) was purified from Streptomyces clavuligerus by a combination of salt precipitation, ultrafiltration, and anion-exchange chromatography. The final purified material gave two protein bands with molecular weights of 283,000 and 32,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Electrophoresis in nondenaturing gels gave a single protein band with an estimated molecular weight of 560,000. These results suggest that ACVS is a multimer composed of nonidentical subunits.
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页码：7269 / 7271
页数：3
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