Isolation of pure anhydrotetracycline oxygenase from Streptomyces aureofaciens
Keyword(s):
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.
1989 ◽
Vol 56
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pp. 391-397
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1983 ◽
Vol 722
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pp. 226-233
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1977 ◽
Vol 83
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pp. 724-738
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1984 ◽
Vol 138
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pp. 144-155
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1985 ◽
Vol 13
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pp. 241-242
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1978 ◽
Vol 146
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pp. 1-32
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