Isolation of pure anhydrotetracycline oxygenase from Streptomyces aureofaciens. |
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Authors: | I Vancurová J Volc M Flieger J Neuzil J Novotná J Vlach V B?hal |
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Affiliation: | Institute of Microbiology, Czechoslovak Academy of Sciences, Prague. |
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Abstract: | Anhydrotetracycline oxygenase was purified to homogeneity from Streptomyces aureofaciens, a producer of tetracycline. The enzyme was purified 60-fold in a 40% yield by a two-step procedure using a combination of hydrophobic chromatography and ion-exchange h.p.l.c. Purified anhydrotetracycline oxygenase was homogeneous according to SDS/polyacrylamide-gel electrophoresis, isoelectric focusing, ion-exchange h.p.l.c. on a Mono Q HR 5/5 column and size-exclusion h.p.l.c. on a TSK G 3000 SW column. The enzyme consists of two subunits of Mr 57,500, as determined by SDS/polyacrylamide-gel electrophoresis. |
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