Purification of isopenicillin N synthetase
- 15 September 1984
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 222 (3), 789-795
- https://doi.org/10.1042/bj2220789
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.Keywords
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