Isolation and Purification of a Diisopropyl Phosphorofluoridate Hydrolase from Thermophilic Bacteria

Abstract

Diisopropylphosphorofluoridate (DPF) hydrolase from thermophilic bacteria has been partially purified by using ammonium sulfate precipitation. This procedure was then followed by various column chromatography isolation techniques - DE-52, phenyl boronate agarose, and phenyl sepharose CL-4B. Further work is needed to purify the enzyme to homogeneity.

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Document Details

Document Type
Technical Report
Publication Date
Apr 01, 1987
Accession Number
ADA180558

Entities

People

  • Lichun H. Walls

Organizations

  • Morgan State University

Tags

Communities of Interest

  • Air Platforms

DTIC Thesaurus Topics

  • Bacteria
  • Chemical Synthesis
  • Chemistry
  • Chromatography
  • Classification
  • Column Chromatography
  • Contracts
  • Electrophoresis
  • Engineering
  • Enzymes
  • Gel Electrophoresis
  • Homogeneity
  • Hydrolases
  • Materials
  • Polysaccharides
  • Precipitation
  • Security

Fields of Study

  • Biology
  • Chemistry

Readers

  • Molecular and Cellular Biochemistry
  • Neurotoxicology