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. 1984 Sep 15;222(3):789–795. doi: 10.1042/bj2220789

Purification of isopenicillin N synthetase.

C P Pang, B Chakravarti, R M Adlington, H H Ting, R L White, G S Jayatilake, J E Baldwin, E P Abraham
PMCID: PMC1144243  PMID: 6435606

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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