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- W164593456 abstract "Ascorbic acid-2-sulfatase was isolated from rat liver by a multistep procedure. DEAE Sephacel ion-exchange chromatography resolved crude ascorbic acid-2-sulfatase into cationic and anionic fractions. These fractions were purified 75- and 230-fold, respectively. The comparative biochemical properties suggest that arylsulfatase B is responsible for the cationic ascorbic acid-2-sulfatase activity, while arylsulfatase A appears to be responsible for the anionic ascorbic acid-2-sulfatase activity. Partially purified arylsulfatase A hydrolyzed ascorbic acid-2-sulfate at 4% the rate of p-nitrocatechol sulfate hydrolysis, while arylsulfatase B hydrolyzed ascorbic acid-2-sulfate at 0.6% the p-nitrocatechol sulfate rate." @default.
- W164593456 created "2016-06-24" @default.
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- W164593456 date "1987-01-01" @default.
- W164593456 modified "2023-10-17" @default.
- W164593456 title "Isolation and Characterization of Rat Hepatic Ascorbic Acid-2-Sulfatases" @default.
- W164593456 doi "https://doi.org/10.1159/000469250" @default.
- W164593456 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2884099" @default.
- W164593456 hasPublicationYear "1987" @default.
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