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B6db references: 79216307

type Journal Article
authors Tanizawa, K.; Soda, K.
title Purification and properties of pig liver kynureninase
journal J Biochem (Tokyo)
ui 79216307
year (1979)
volume 85
number 4
pages 901-6.
keywords Animal
abstract Kynureninase [L-kynurenine hydrolase, EC] was purified from pig liver by a procedure including DEAE-cellulose chromatography, hydroxyapatite chromatography, ammonium sulfate fractionation, DEAE-Bio Gel chromatography, Sephacryl S-200 gel filtration, kynurenine- Sepharose affinity chromatography, and Sephadex G-200 gel filtration. The enzyme was found to be homogeneous by the criterion of disc-gel electrophoresis. The enzyme has a molecular weight of about 100,000 and exhibits absorption maxima at 280 and 420 nm. The optimum pH and the isoelectric point of the enzyme are 8.5 and 5.0, respectively. The Michaelis constants were determined to be as follows: L-kynurenine, 7.7 X 10(-4) M; L-3-hydroxykynurenine, 1.3 X 10(-5) M; and pyridoxal 5'- phosphate, 1.8 X 10(-6) M. L-3-Hydroxykynurenine is hydrolyzed more rapidly than L-kynurenine; the liver enzyme can be regarded as a 3- hydroxy-kynureninase.
last changed 2002/11/12 16:17

B6db references