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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Isolation and characterization of rat hepatic ascorbic acid-2-sulfatases. Thompson, D.B., Daniel, W.L. Enzyme (1987) [Pubmed]
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