Amine Oxidases of Microorganisms Part IV. Further Properties of Amine Oxidase of Aspergillus niger
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چکیده
There was an increase in copper content proportional to the increase in specific activity of the enzyme during the purification of amine oxidase of Aspergillus niger. The recrystal lized enzyme preparation contained 1 g atom of copper per 83,000g of protein. This in dicated that the enzyme contained 3g atoms of copper per mole of enzyme. The copper in the enzyme was removed by dialysis against sodium diet hyldithiocarbamate with con comitant loss of activity. The dialyzed enzyme was reactivated by the addition of cupric copper. The copper in the enzyme was present in cupric state. No valency change of the copper was observed in the catalytic activity. The enzyme was inhibited by various chelating agents, and potently inhibited by various carbonyl reagents.
منابع مشابه
Amine Oxidases of Microorganisms Part II. Purification and Crystallization of Amine Oxidase of Aspergillus niger
A procedure for obtaining crystalline preparations of the amine oxidase of Aspergillus niger has been developed. The method involved fractionations with ammonium sulfate and separation on successive columns of DEAE-cellulose, DEAE-sephadex and hydroxyl apatite. Crystals were formed when solid ammonium sulfate was added to solutions of the purified enzyme (of about 300to 350-times the specific a...
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