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Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina

A highly active organophosphorus acid anhydrolase from Alteromonas undina was purified to homogeneity and found to be composed of a single polypeptide chain with a molecular weight of 53,000. With diisopropylfluorophosphate as a substrate, the purified enzyme has a specific activity of ∼575 μmol/min...

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Detalhes bibliográficos
Main Authors: Cheng, Tu-Chen, Harvey, Steven P., Stroup, Adam N.
Formato: Artigo
Idioma:Inglês
Publicado em: 1993
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC182420/
https://ncbi.nlm.nih.gov/pubmed/16349054
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