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      A pure enzyme catalyzing penicillin biosynthesis.

      Science (New York, N.Y.)
      Acremonium, enzymology, Chromatography, Gel, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Enzymes, isolation & purification, metabolism, Oxidoreductases, Penicillins, biosynthesis

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          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 degrees C for several weeks without any loss in activity.

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