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