title: Purification and partial characterization of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Streptomyces clavuligerus.
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.
authors: Department of Microbiology, University of Alberta, Edmonton, Canada.
authors: S E
authors: SE
authors: Jensen
authors: A
authors: A
authors: Wong
authors: M J
authors: MJ
authors: Rollins
authors: D W
authors: DW
authors: Westlake
mesh_terms: D002845:Chromatography; D008970:Molecular Weight; D010453:Peptide Synthases / Q000302:isolation & purification*; D013302:Streptomyces / Q000201:enzymology*
chemical_list: D010453:Peptide Synthases; C095368:alpha-aminoadipyl-cysteinyl-valine synthetase