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  • Title: Purification of isopenicillin N synthetase.
    Author: Pang CP, Chakravarti B, Adlington RM, Ting HH, White RL, Jayatilake GS, Baldwin JE, Abraham EP.
    Journal: Biochem J; 1984 Sep 15; 222(3):789-95. PubMed ID: 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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