Abstract

This chapter discusses the methods of preparation of amine oxidase ( Aspergillus niger ). Amine oxidase catalyzes the oxidative deamination of various amines and produces the corresponding aldehydes, ammonia, and hydrogen peroxide, stoichiometrically. The spectrophotometric assay described in chapter is based on the measurement of' benzaldehyde during the oxidation of benzylamine. The spectrophotometric unit of amine oxidase activity is defined as that quantity of enzyme that produces an initial rate of change of 0.001 per minute in the optical density at 250 mμ. Specific activity is expressed as spectrophotometric units per milligram of protein. The protein is determined by measuring the absorbancy at 280 mμ. The crystalline enzyme can be stored at 0-5 ° as a suspension in 0.06 M phosphate buffer, pH 6.5, containing 30% saturated ammonium sulfate. The specific and total activity of the enzyme remains constant for periods of over 5 months. The enzyme exhibits absorption maxima at about 280 and 480-500 mμ. A shoulder at 410 mμ, is also noted in the spectrum. The pink color of the enzyme is related to the maximum around 480 mμ.

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