Amine Oxidases of Microorganisms Part II. Purification and Crystallization of Amine Oxidase of Aspergillus niger
نویسندگان
چکیده
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 activity of the crude mycelium extract). The crystals appeared as fine rods, with a faint pink color. The crystals had a specific activity around 10,000 which was about 20 times as active as that of crystalline preparations of the animal monoamine oxidase.
منابع مشابه
Competitive inhibition of copper amine oxidases by vitamin B hydrochloride in chickpea
Copper amine oxidases (CAOs) catalyse the oxidative de-amination of biogenic amines which are ubiquitous compounds essential for cell growth and proliferation. The enzymes are homodimers containing both topaquinone and a Cu(II) ions as cofactors at the active site of each subunit. After extraction and purification of chickpea (cicer arietinum) amine oxidase by chromatoghraphy, Km and Vmax of th...
متن کاملAmine Oxidases of Microorganisms Part IV. Further Properties of Amine Oxidase of Aspergillus niger
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 ...
متن کاملInhibition of chickpea seedling copper amine oxidases by tetraethylenepentamine
Copper amine oxidases are important enzymes, which contribute to the regulation of mono- and polyamine levels. Each monomer contains one Cu(II) ion and 2,4,5-trihydroxyphenylalanine (TPQ) as cofactors. They catalyze the oxidative deamination of primary amines to aldehydes with a ping-pong mechanism consisting of a transamination. The mechanism is followed by the transfer of two electrons to mol...
متن کاملPurification and Properties of the Glucose Oxidase from Aspergillus Niger.
Glucose oxidase (/3-n-glucose : 02 oxidoreductase, EC 1.1.3.4) has been highly purified from the extracts of three fungi, Penicillium not&urn (1, 2), Penicillium amagasakiense (3, 4), and Aspergillus niger (5, 6). It has also been identified and sometimes partially purified from a number of other sources. Some of these sources are reviewed by Schepartz and Subers (7). Recently Pazur and Kleppe ...
متن کاملPartition of Glucose Oxidase from Aspergillus niger in Aqueous Two-Phase Systems Based on Salt and Polyethylene Glycol
The aim of this work was to study the isolation of glucose oxidase (GOx) from Aspergillus niger in aqueous two phase system consisting of PEG 7500 (150g l), potassium phosphate (175 g l, K2HPO4 +KH2PO4) and glucose (10 gl), the enzyme was partitioned in polymer phase. By sequential extraction GOx (69.2%) was recovered in polymer phase by 11.8 fold purification, giving a yield of 129U mg protein-.
متن کامل