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Formation in vitro of ascorbic acid 2-sulfate

M Mohamram, R B Rucker, R E Hodges

    Biochimica Et Biophysica Acta
    |June 23, 1976
    PubMed
    Summary

    Researchers investigated ascorbic acid sulfation using rat liver and colon enzymes. Ascorbic acid 2-sulfate was formed, requiring ATP and influenced by specific inhibitors, with vitamin A deficiency showing minimal impact.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Nutritional Science

    Background:

    • Ascorbic acid (vitamin C) is essential for numerous physiological processes.
    • Sulfation is a key metabolic modification for various biomolecules.
    • The enzymatic pathways for ascorbic acid sulfation were not fully elucidated.

    Purpose of the Study:

    • To investigate the enzymatic sulfation of ascorbic acid in rat liver and colon homogenates.
    • To identify the specific sulfated metabolite formed and the required cofactors.
    • To assess the influence of vitamin A status on this sulfation process.

    Main Methods:

    • Utilized rat liver and colon homogenates as enzyme sources.
    • Employed radioactive sulfate (Na2 35SO4) and 3'-phosphoadenylyl [35S]sulfate (P-Ado-P-35S) as sulfate donors.
    • Analyzed reaction products using thin-layer cellulose chromatography.
    • Investigated the role of ATP and ATP sulfurylase inhibitors.
    • Compared enzyme activity in vitamin A deficient and sufficient rats.

    Main Results:

    • Ascorbic acid 2-sulfate was identified as the primary sulfated product.
    • Adenosine triphosphate (ATP) was confirmed as an obligatory cofactor for sulfation when using Na2 35SO4.
    • ATP sulfurylase inhibitors reduced the incorporation of [35S]sulfate into ascorbic acid 2-sulfate.
    • P-Ado-P-35S served as a potent sulfating agent in the absence of ATP.
    • Vitamin A deficiency had a negligible effect on ascorbic acid 2-sulfate formation.

    Conclusions:

    • Rat liver and colon possess an ascorbic acid sulphotransferase activity.
    • The sulfation pathway likely involves ATP-dependent activation of inorganic sulfate.
    • Ascorbic acid 2-sulfate is the principal product of this enzymatic reaction.
    • Vitamin A status does not appear to significantly modulate ascorbic acid sulfation in these tissues.

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