| http://purl.uniprot.org/citations/2884099 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2884099 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/2884099 | http://purl.org/dc/terms/identifier | "doi:10.1159/000469250"xsd:string |
| http://purl.uniprot.org/citations/2884099 | http://purl.uniprot.org/core/author | "Thompson D.B."xsd:string |
| http://purl.uniprot.org/citations/2884099 | http://purl.uniprot.org/core/author | "Daniel W.L."xsd:string |
| http://purl.uniprot.org/citations/2884099 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/2884099 | http://purl.uniprot.org/core/name | "Enzyme"xsd:string |
| http://purl.uniprot.org/citations/2884099 | http://purl.uniprot.org/core/pages | "134-140"xsd:string |
| http://purl.uniprot.org/citations/2884099 | http://purl.uniprot.org/core/title | "Isolation and characterization of rat hepatic ascorbic acid-2-sulfatases."xsd:string |
| http://purl.uniprot.org/citations/2884099 | http://purl.uniprot.org/core/volume | "37"xsd:string |
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