Abstract
Summary The preparation of crystalline kynureninase from Pseudomonas marginalis is described. The enzyme is homogeneous by the criteria of ultra-centrifugation and disc gel electrophoresis. The molecular weight is 100,000 and 1 mole of pyridoxal 5′-phosphate is bound per mole of enzyme as a coenzyme. The enzyme exhibits absorption maxima at 280, 337 and 430 mμ. The coenzyme is resolved from the enzyme by the treatment with hydroxylamine or L-alanine.
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