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Purification and properties of threonine dehydratase from Rhodopseudomonas spheroides

✍ Scribed by G.J. Barritt; J.F. Morrison


Book ID
115732865
Publisher
Elsevier Science
Year
1972
Weight
801 KB
Volume
284
Category
Article
ISSN
0005-2744

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Threonine dehydratase has been purified about 200-fold from extracts of Candida maltosa by chromatography on DEAE-cellulose, Sephadex G-200, and hydroxylapatite. The enzyme is fairly stable in solution in the presence of 250 mM phosphate buffer containing 40% glycerol. The molecular weight of the na