title: Partial purification and characterization of anhydrotetracycline oxygenase of Streptomyces aureofaciens.
abstract: 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 isoelectric 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.
mesh_terms: D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008970:Molecular Weight; D010105:Oxygenases / Q000032:analysis / Q000302:isolation & purification*; D013304:Streptomyces aureofaciens / Q000201:enzymology*
chemical_list: D010105:Oxygenases; C034689:anhydrotetracycline oxygenase