[Partial purification and characterization of a D-amino acid oxidase from the hepatopancreas of Octopus vulgaris].
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.
D010129:4-Aminobenzoic Acid / Q000494:pharmacology; D000818:Animals; D001565:Benzoates / Q000494:pharmacology; D019817:Benzoic Acid; D002850:Chromatography, Gel; D003605:D-Amino-Acid Oxidase / Q000302:isolation & purification*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology; D008970:Molecular Weight; D049831:Octopodiformes / Q000201:enzymology*; D010179:Pancreas / Q000201:enzymology
D001565:Benzoates; D005182:Flavin-Adenine Dinucleotide; D019817:Benzoic Acid; D003605:D-Amino-Acid Oxidase; D010129:4-Aminobenzoic Acid
Purificazione parziale e caratterizzazione di una D-aminoacido ossidasi da epatopancreas di Octopus vulgaris.