A Pure Enzyme Catalyzing Penicillin Biosynthesis
- 11 May 1984
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 224 (4649) , 610-612
- https://doi.org/10.1126/science.6546810
Abstract
Isopenicillin N synthetase (cyclase) has been purified to homogeneity from Cephalosporium acremonium strain C-10. The enzyme has a molecular weight of 40,000 to 42,000 and yields a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme was purified in 10 percent yield by a combination of protamine sulfate and ammonium sulfate precipitations, gel filtration, and ion-exchange high-performance liquid chromatography. The purified enzyme can be stabilized with sucrose and stored at -20°C for several weeks without any loss in activity.This publication has 13 references indexed in Scilit:
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