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  • Title: Copurification of L-ascorbate-2-sulfate sulfohydrolase and arylsulfatase activities from the liver of a marine gastropod, Charonia lampas.
    Author: Hatanaka H, Ogawa Y, Egami F.
    Journal: J Biochem; 1975 Feb; 77(2):353-9. PubMed ID: 236288.
    Abstract:
    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.
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