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Isolation and characterization of rat hepatic ascorbic acid-2-sulfatases.

Authors: Thompson, DB  Daniel, WL 
Citation: Thompson DB and Daniel WL, Enzyme. 1987;37(3):134-40.
Pubmed: (View Article at PubMed) PMID:2884099

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.


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RGD Object Information
RGD ID: 1599231
Created: 2007-01-22
Species: All species
Last Modified: 2007-01-22
Status: ACTIVE


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