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. 1973 Nov;116(2):857–866. doi: 10.1128/jb.116.2.857-866.1973

Cyclic 3′,5′-Adenosine Monophosphate Phosphodiesterase of Escherichia coli

L D Nielsen a, D Monard a,1, H V Rickenberg a
PMCID: PMC285456  PMID: 4355491

Abstract

The cyclic 3′,5′-adenosine monophosphate (c-AMP) phosphodiesterase from Escherichia coli has been partially purified. The enzyme has an apparent molecular weight of 30,000, a Michaelis constant of 0.5 mM c-AMP, and a pH optimum of 7. The partially purified enzyme requires for activity the presence of a reducing compound and of either iron or a protein which seemingly acts as iron carrier.

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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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