Plasma Amine Oxidase
Plasma amine oxidase (PAO) catalyzes the reaction:
RCH2NH2 + O2 + H2O → RCHO + NH3 + H2O2
Bovine plasma amine oxidase has a molecular weight of 170 kDa and an optimum pH of 6.2 for spermine and 7.2 for spermidine. Amine oxidases are divided into two classes: the pyridoxal and copper containing enzyme to which plasma amine oxidase belongs, and the FAD-containing amino oxidases. Natural substrates include catecholamines, tryptamine derivatives and other physiologically active amines. Plasma amine oxidase is used in research requiring nitrogen group transfers. The molecule is composed of two identical polypeptide chains. There are two pyridoxal phosphates and two atoms of Cu+ per molecule. Bovine plasma amine oxidase is inhibited by copper chelating agents, many carboxyl reagents such as cuprizone, hydroxylamine and cyanide. Benzoic acid and benzyl alcohol are both non-competitive inhibitors (KI = 30 and 34mM respectively). The assay for determination of amine oxidases employed at Worthington is essentially that of Tabor et al., JBC, 208, 645, (1954) with the reaction temperature reduced to 25°C.
Stability/Storage: Stable for 12 months at -20°C. Store at -20°C.
Technical Note: 1 I.U. equals 4,330 Tabor units. (T.U.)
The assay method at Worthington is that of Tabor (1954) where one unit results in the oxidation of one micromole of benzylamine per minute at 25°C, pH 7.2. under the specified conditions. 4,330 Tabor units is equivalent to one International Unit.