title: Purification of isopenicillin N synthetase.
abstract: Isopenicillin N synthetase was extracted from Cephalosporium acremonium and purified about 200-fold. The product showed one major protein band, coinciding with synthetase activity, when subjected to electrophoresis in polyacrylamide gel. An isopenicillin N synthetase from Penicillium chrysogenum was purified about 70-fold by similar procedures. The two enzymes resemble each other closely in their Mr, in their mobility on electrophoresis in polyacrylamide gel and in their requirement for Fe2+ and ascorbate for maximum activity. Preliminary experiments have shown that a similar isopenicillin N synthetase can be extracted from Streptomyces clavuligerus.
mesh_terms: D000164:Acremonium / Q000201:enzymology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004798:Enzymes / Q000302:isolation & purification*; D010088:Oxidoreductases; D010408:Penicillium chrysogenum / Q000201:enzymology; D013302:Streptomyces / Q000201:enzymology
chemical_list: D004798:Enzymes; D010088:Oxidoreductases; C038370:isopenicillin N synthetase