Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 11 May 1984:
Vol. 224. no. 4649, pp. 610 - 612
DOI: 10.1126/science.6546810
Prev | Table of Contents | Next

Articles

Science, Vol 224, Issue 4649, 610-612
Copyright © 1984 by American Association for the Advancement of Science

articles

A pure enzyme catalyzing penicillin biosynthesis

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

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Molecular Regulation of beta -Lactam Biosynthesis in Filamentous Fungi.
A. A. Brakhage (1998)
Microbiol. Mol. Biol. Rev. 62, 547-585
   Abstract »    Full Text »    PDF »
Enzymatic approach to syntheses of unnatural beta-lactams.
S Wolfe, A. Demain, S. Jensen, and D. Westlake (1984)
Science 226, 1386-1392
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)