| Literature DB >> 2254285 |
S E Jensen1, A Wong, M J Rollins, D W Westlake.
Abstract
delta-(L-alpha-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.Entities:
Mesh:
Substances:
Year: 1990 PMID: 2254285 PMCID: PMC210854 DOI: 10.1128/jb.172.12.7269-7271.1990
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490