[Isolation and various characteristics of tryptophan deaminase from Proteus vulgaris].
Tryptophan deaminase was isolated from Proteus vulgaris and purified. The procedure for enzyme purification included the cell destruction on USD-1, fractionation by ammonium sulphate, gel chromatography on ultragel AcA34, ion exchange chromatography on DEAE-cellulose. A degree of the enzyme purification--95, yield--5.7%. The pH optimum was 7.5, the temperature optimum--47 degrees C. The enzyme molecular weight (105 kD) was estimated by gel chromatography on Sephadex G-200, Km--5.0 mM in the K-phosphate buffer (pH 7.5). The SH groups are supposed to be present in the active site of the enzyme. The enzyme does not accelerate oxidation deamination of phenylalanine and tyrosine.
Pimenova
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EI
D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006863:Hydrogen-Ion Concentration; D050830:L-Amino Acid Oxidase; D008970:Molecular Weight; D011514:Proteus vulgaris / Q000201:enzymology*; D013696:Temperature
D000594:Amino Acid Oxidoreductases; D050830:L-Amino Acid Oxidase
Vydelenie i nekotorye kharakteristiki triptofandezaminazy Proteus vulgaris.