Purification and characterization of amine oxidase from soybean seedlings
1993
Vianello, F. | Di Paolo, M.L. | Stevanato, R. | Gasparini, R. | Rigo, A.
A simple and rapid procedure for purification of soybean seedling amine oxidase is reported. The crude enzyme, obtained by ammonium sulfate fractionation was purified by ion-exchange chromatography on a cellulose phosphate column and batch affinity chromatography on 6-aminohexyl-Sepharose. Cyclohexylamine, a competitive inhibitor, was utilized to elute the enzyme. A homogeneous enzyme was obtained with a yield higher than 25%, the content of minor components being less than or equal to 2%. The M(r) estimated by gel filtration is 113,000 and 77,000 by sodium lauryl sulfate-polyacrylamide gel electrophoresis. The enzyme is a dimer and contains two Cu(2+) ions per molecule. Its EPR spectrum is typical of Cu(2+) in a tetragonal symmetry. The enzyme oxidizes cadaverine at high rate, the specific activity being 4.3 microkat/mg. Molecular, spectroscopic, and kinetic properties of this enzyme are reported.
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