Abstract
The distribution of choline oxidase activity was studied with cell-free extracts of yeasts, molds and actinomycetes. A fungus which was identified as Cylindrocarpon didymum M–1 showed the highest activity. The enzyme was purified from the cell-free extract of C. didymum M–1 by a procedure involving ammonium sulfate fractionation and DEAE-cellulose, hydroxyl-apatite and Sephadex G–150 column chromatographies. The enzyme preparation was homogeneous when subjected to disc gel electrophoresis and ultracentrifugation. Sedimentation velocity yielded a value of . The enzyme showed a typical flavoprotein spectrum of absorption maxima at 276,370 and 454 nm.
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