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dc.contributor.authorBenitez, Lita V.
dc.contributor.authorHalver, John E.
dc.identifier.citationBenitez, L.V., & Halver, J.E. (1982). Ascorbic acid sulfate sulfohydrolase (C2 sulfatase): the modulator of cellular levels of L-ascorbic acid in rainbow trout. Proceedings of the National Academy of Sciences, 79(18), 5445-5449.en
dc.description.abstractThe enzyme L-ascorbic acid 2-sulfate sulfohydrolase (C2 sulfatase) was purified from rainbow trout liver. The enzyme catalyzes the hydrolysis of L-ascorbic acid 2-sulfate and has a pH optimum at 6.0. It has a molecular weight of about 117,500 at pH 5.0 and is inhibited by a number of sulfhydryl blocking agents including L-ascorbic acid. C2 sulfatase activity was observed in most metabolic organs of rainbow trout. These findings suggest that the physiologic role of the enzyme is to maintain adequate cellular concentrations of L-ascorbic acid in the fish. The activity of the enzyme is controlled by L-ascorbic acid through feedback inhibition. Comparison of kinetic constants and inhibition patterns suggests that C2 sulfatase is structurally identical to human arylsulfatase A. However, unlike C2 sulfatase, human arylsulfatase A may not be involved in ascorbate metabolism. Its physiologic substrate is reported to be cerebroside-3-sulfate, not L-ascorbic acid 2-sulfate. A scheme is proposed to account for the functional divergence of these two structurally identical enzymes.en
dc.description.sponsorshipThis work was supported by the Southeast Asian Fisheries Development Center (SEAFDEC-IDRC MILKFISH PHASE II-3P-78-0033) and Washington Sea Grant (LARVAL FEED-61-8918). This is contribution no. 590, School of Fisheries, University of Washington, Seattle.en
dc.publisherNational Academy of Sciences of the United States of Americaen
dc.subjectAscorbic acid sulfataseen
dc.subjectEnzymatic activityen
dc.subjectFish cultureen
dc.subjectSalmo gairdnerien
dc.titleAscorbic acid sulfate sulfohydrolase (C2 sulfatase): the modulator of cellular levels of L-ascorbic acid in rainbow trout.en
dc.citation.journalTitleProceedings of the National Academy of Sciencesen

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  • AQD [1129]
    These papers were contributed by AQD staff to various national and international journals

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