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The apoenzyme of d-aspartate oxidase from Cryptococcus humicolus UJ1 was obtained by dialyzing the holoenzyme against 3 M KBr in 250 mM potassium phosphate (pH 7.0), 0.3 mM EDTA and 5 mM 2-mercaptoethanol, followed by gel filtration on Superdex 200 to separate from the remaining holoenzyme. Apo-d-aspartate oxidase is entirely present as a monomeric protein of 40 kDa, while the reconstituted holoenzyme...
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