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

@article{Cheng1993PurificationAP,
  title={Purification and Properties of a Highly Active Organophosphorus Acid Anhydrolase from Alteromonas undina.},
  author={Timothy C. Cheng and Steven P Harvey and Alice Stroup},
  journal={Applied and environmental microbiology},
  year={1993},
  volume={59 9},
  pages={3138-40}
}
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 approximately 575 mumol/min/mg of protein. The enzyme has optimum activity at pH 8.0 and 55 degrees C and is stimulated by sulfhydryl reducing agents and manganese. It is capable of rapidly hydrolyzing a wide… CONTINUE READING

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