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Partial purification and characterization of anhydrotetracycline oxygenase of Streptomyces aureofaciens

✍ Scribed by Ivana Vančurová; Miroslav Flieger; Jindřich Volc; Milan J. Beneš; Jana Novotná; Jiří Neužil; Vladislav Běhal

Publisher
John Wiley and Sons
Year
1987
Tongue
English
Weight
310 KB
Volume
27
Category
Article
ISSN
0233-111X

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✦ Synopsis

Anhydrotetracycline oxygenase was purified both by affinity chromatography and by hydrophobic interaction chromatography. Molecular weight of anhydrotetracycline oxygenase was determined to be 115,000 by Sephadex G-200 gel filtration. Using preparative jsoelectric focusing the isoelectric point of the enzyme was estimated to be 5.3. The enzyme showed a sensitivity to thiol-specific inhibitors. During the hydrophobic interaction purification step, the activity dropped considerably. Reactivation occurred when a heat treated crude extract was added to the reaction mixture.

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