| Abstract: | Partial purification and characterization of a D-aminoacid oxidase from Octopus vulgaris hepatopancreas are described. An about 25-fold purification was achieved. The pH optimum was near to 9; molecular weight, determined by gel-filtration through G 200 Sephadex was approximately 55000; apparent Km was 10(-3)M. The enzyme showed great affinity for D-Ala and D-Val. Recovery of activity, due to pre-incubation with FAD was observed. The enzyme is strongly inhibited by benzoic acid and moderately inhibited by p-aminobenzoic acid. |
