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. 1965 Aug;90(2):380–383. doi: 10.1128/jb.90.2.380-383.1965

Enzymatic Deacylation of S35-Benzylpenicillin

David L Pruess 1, Marvin J Johnson 1
PMCID: PMC315654  PMID: 14329451

Abstract

Pruess, David L. (University of Wisconsin, Madison), and Marvin J. Johnson. Enzymatic deacylation of S35-benzylpenicillin. J. Bacteriol. 90:380–383. 1965.—S35-benzylpenicillin, penicilloic acid, and penilloic acid were deacylated by cell suspensions of Escherichia coli and Micrococcus roseus. Both cultures deacylated penicillin most rapidly and penilloic acid least rapidly. The deacylase activity of M. roseus against penicilloic acid was cell-bound, probably requiring a metal ion for activity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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