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D-Amino Acid Oxidase, Porcine Kidney (D-AAO, D-Amino acid: oxygen oxidoreductase, deaminating, DAO, OXDA)

Cat no: A1373

Supplier: United States Biological
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D-Amino Acid Oxidase is a flavoprotein oxidase, flavin being the only prosthetic group. The enzyme from porcine kidney has been extensively studied. It is isolated as a stable crystalline complex with benzoate, from which the holo and apoenzyme may be prepared. The benzoate is readily exchanged for a substrate. Enzyme Commission (EC) Number: (BRENDA | IUBMB ) MDL number: MFCD00081546 EG/EC Number: 232-563-5 Source: Porcine kidney Form: Supplied as a lyophilized powder. Activity: (same/more than)1.5 units/mg Protein Unit Definition: 1 unit oxidizes 1umole of D-alanine per minute @ 37 degrees C, pH 8.3. Quality Control: SDS-PAGE Unit Definition: One unit will oxidatively deaminate 1umole of D-alanine to pyruvate per minute at pH 8.3 at 25 degrees C, in the presence of a catalase. Storage and Stability: 6 months at -20 degrees C
Catalogue number: A1373
Size: 100U
Alternative names: EC=; Porcine Kidney
References: 1. Bright, H., and Porter, D.: in The Enzymes, XII, Pt. B, 3rd ed., (Boyer, P., ed.), Academic Press, NY, 445 (1975). 2. Curti, B., Ronchi, S., Branzoli, U., Ferri, G., and Williams, C.: Improved Purification, Amino Acid Analysis and Molecular Weight of Homogeneous D-Amino Acid Oxidase from Pig Kidney, Biochim. Biophys. Acta, 327, 266 (1973). 3. Dixon, M., and Kleppe, K.: D-Amino Acid Oxidase. I. Dissociation and Recombination of the Holoenzyme, Biochim. Biophys. Acta, 96, 357 (1965a). 4. Tu, S., and McCormick, D.: Photoinactivation of Porcine D-Amino Acid Oxidase with Flavin Adenine Dinucleotide, J. Biol. Chem., 248, 6339 (1973). 5. Tu, S., Edelstein, S., and McCormick, D.: A Modified Purification Method and Properties of Pure Porcine D-Amino Acid Oxidase, Arch. Biochem. Biophys., 159, 889 (1973). 6. Yagi, K., and Natsume, K.: Inhibitory Action of Pyruvate on D-Amino Acid Oxidase, J. Biochem. Japan, 55, 529 (1964). 7. Yagi, K., and Okamura, K.: Isolation by Crystallization of Fully Reduced D-Amino Acid Oxidase, Biochem. Biophys. Res. Comm., 21, 399 (1965a).

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