Copurification of L-ascorbate-2-sulfate sulfohydrolase and arylsulfatase activities from the liver of a marine gastropod, Charonia lampas.
Ascorbate-2-sulfate sulfohydrolase was purified 184-fold from a crude extract of the liver of Charonia lampas.  In all purification steps including phosphocellulose, first and second Sephadex G-150 column chromatographies, the enzyme activity eluted together with arylsulfatase [ED 3.1.6.1] activity, and was separated from glycosulfatase ]EC 3.1.6.3] activity.  The nonidentity of ascorbate-2-sulfate sulfohydrolase and glycosulfatase was further confirmed by an isoelectric focussing study.  Ascorbate-2-sulfate sulfohydrolase had an isoelectric point, pI, of 4.9, and had maximum activity at pH 4.0.  Its molecular weight was estimated to be about 154.000.
D000818:Animals; D001192:Arylsulfatases / Q000302:isolation & purification* / Q000378:metabolism; D001205:Ascorbic Acid; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005947:Glucose; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D008974:Mollusca / Q000201:enzymology*; D009596:Nitrophenols; D013429:Sulfatases / Q000302:isolation & purification*
D009596:Nitrophenols; D013429:Sulfatases; D001192:Arylsulfatases; D005947:Glucose; D001205:Ascorbic Acid