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Purification and properties of D-gluconate dehydratase fromAchromobacter

✍ Scribed by K. Kersters; Junko Khan-Matsubara; L. Nelen; J. Ley

Publisher
Springer Netherlands
Year
1971
Tongue
English
Weight
691 KB
Volume
37
Category
Article
ISSN
0003-6072

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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