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 [EC 3.1.6.1] activity,...

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Bibliographic Details
Published inJournal of biochemistry (Tokyo) Vol. 77; no. 2; pp. 353 - 359
Main Authors HATANAKA, Hiroshi, OGAWA, Yoko, EGAMI, Fujio
Format Journal Article
LanguageEnglish
Published England Oxford University Press 01.02.1975
Subjects
Animals
Arylsulfatases - isolation & purification
Arylsulfatases - metabolism
Ascorbic Acid
Chromatography, Gel
Chromatography, Ion Exchange
Glucose
Hydrogen-Ion Concentration
Isoelectric Focusing
Kinetics
Liver - enzymology
Molecular Weight
Mollusca - enzymology
Nitrophenols
Sulfatases - isolation & purification
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Summary: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.
Bibliography:istex:6DB1CF6A7CCDF91DEA564329E2468FE5400D14F8
ark:/67375/HXZ-ZMJCR8WZ-Z
ArticleID:77.2.353
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a130732