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PMID: 6546810 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

A pure enzyme catalyzing penicillin biosynthesis.

Science (New York, N.Y.) ·Vol. 224 ·No. 4649 ·1984-05-11 ·Pages 610-2

Hollander IJ, Shen YQ, Heim J, Demain AL, Wolfe S

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.

MeSH Terms
Acremonium/enzymology Chromatography, Gel Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Enzymes/isolation & purification,metabolism Oxidoreductases Penicillins/biosynthesis
Chemicals
Enzymes Penicillins Oxidoreductases isopenicillin N synthetase penicillin N
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Hollander I J
Shen Y Q
Heim J
Demain A L
Wolfe S
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1984-05-11
Pages
610-2
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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