Copurification of L-Ascorbate-2-sulfate Sulfohydrolase and Arylsulfatase Activities from the Liver of a Marine Gastropod, Charonia lampas
- 1 February 1975
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 77 (2) , 353-359
- https://doi.org/10.1093/oxfordjournals.jbchem.a130732
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 [EC 3.1.6.1] activity, and was separated from glycosul-fatase [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.Keywords
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