title: Isolation and characterization of rat hepatic ascorbic acid-2-sulfatases.
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.
mesh_terms: D000818:Animals; D001192:Arylsulfatases / Q000302:isolation & purification*; D001205:Ascorbic Acid / Q000031:analogs & derivatives; D002396:Catechols; D002553:Cerebroside-Sulfatase / Q000302:isolation & purification; D002803:Chondro-4-Sulfatase / Q000302:isolation & purification; D002852:Chromatography, Ion Exchange; D006923:Hymecromone / Q000031:analogs & derivatives; D008099:Liver / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity; D013429:Sulfatases / Q000302:isolation & purification*
chemical_list: D002396:Catechols; C019492:4-methylumbelliferyl sulfate; C001956:ascorbic acid 2-sulfate; D006923:Hymecromone; D013429:Sulfatases; D001192:Arylsulfatases; D002553:Cerebroside-Sulfatase; D002803:Chondro-4-Sulfatase; C021228:4-nitrocatechol sulfate; D001205:Ascorbic Acid