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- W1980967519 abstract "Abstract The d -amino acid oxidase in sonicates of Trigonopsis variabilis was purified by precipitating it with acetone and with ammonlum sulfate, removing nucleo-proteins with protamine sulfate, adsorbing impurities with charcoal, and applying gel and ion-exchange chromatography. The final fraction had a specific activity over 250 times greater than that of the initial sonicate. At 38°C, toluic and benzoic acids did not inhibit the enzyme appreciably, but heating to 55°C for 5 min completely inactivated it. Inhibition by p-chloromercuribenzoate and its partial reversal by 2-mercaptoethanol indicated the probable presence of functional sulfhydryl groups. Addition of FAD did not markedly enhance the activity of the purified enzyme, presumably because the FAD originally present was too tightly bound to permit excessive loss in the purification steps. The apparent Michaelis constant of the purified enzyme for d -leucine approximated 2.8 × 10−4 m . In descending order, activities toward the several d -amino acids tested were: d -leucine > d -tryptophan > d -methionine > d -histidine > d -alanine. The purified enzyme did not attack d -threonine." @default.
- W1980967519 created "2016-06-24" @default.
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- W1980967519 date "1976-03-01" @default.
- W1980967519 modified "2023-10-14" @default.
- W1980967519 title "Purification of d-amino acid oxidase from Trigonopsis variabilis" @default.
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- W1980967519 doi "https://doi.org/10.1016/0003-2697(76)90030-0" @default.
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