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. 1988 Jul 1;253(1):263–267. doi: 10.1042/bj2530263

Isolation of pure anhydrotetracycline oxygenase from Streptomyces aureofaciens.

I Vancurová 1, J Volc 1, M Flieger 1, J Neuzil 1, J Novotná 1, J Vlach 1, V Bĕhal 1
PMCID: PMC1149284  PMID: 3138982

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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Selected References

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