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Arylsulfatase from Streptomyces griseorubiginosus S980-14
1Bristol-Myers Squibb Research Institute, Tokyo, Japan.
Bioscience, Biotechnology, and Biochemistry
|June 1, 1995
Abstract:
A new arylsulfatase designated Es-1, which desulfated etoposide 4'-sulfate and p-nitrophenyl sulfate, was isolated from Streptomyces griseorubiginosus S980-14 and purified to protein homogeneity by ammonium sulfate fractionation, ion exchange column chromatography, and chromatofocusing. The enzyme was active in monomeric form with an approximate molecular weight of 45,000, had a pI value of 4.95, and required calcium for full activity. At an optimum reaction pH of 8.5, iodoacetate, mercurous chloride, and EDTA severely inhibited the activity of Es-1 arylsulfatase.