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.
Purification of isopenicillin N synthetase
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C P Pang, B Chakravarti, R M Adlington, H H Ting, R L White, G S Jayatilake, J E Baldwin, E P Abraham; Purification of isopenicillin N synthetase. Biochem J 15 September 1984; 222 (3): 789–795. doi: https://doi.org/10.1042/bj2220789
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