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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.

SUBMITTER: Pang CP

PROVIDER: S-EPMC1144243 | biostudies-other | 1984 Sep

REPOSITORIES: biostudies-other

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Photoaffinity labelling of isopenicillin N synthetase by laser-flash photolysis.

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