Isolation and Purification of a Diisopropyl Phosphorofluoridate Hydrolase from Thermophilic Bacteria
Technical Report,01 Jun 1986,30 Nov 1986
MORGAN STATE UNIV BALTIMORE MD BALTIMORE
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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.