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17-Hydroxyprogesterone Acetate

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17-Hydroxyprogesterone Acetate – Free Register to Access Experts & Abstracts

Arthur W. Bull – One of the best experts on this subject based on the ideXlab platform.

Sonja M. Earles – One of the best experts on this subject based on the ideXlab platform.

  • Metabolism of oxidized linoleic acid: characterization of 13-hydroxyoctadecadienoic acid dehydrogenase activity from rat colonic tissue.
    Biochimica et biophysica acta, 1991
    Co-Authors: Sonja M. Earles, Joel C. Bronstein, David L. Winner, Arthur W. Bull
    Abstract:

    An oxidized derivative of linoleic acid, 13-hydroxyoctadecadienoic acid (13-HODE), is dehydrogenated by an NAD+ dependent dehydrogenase present in rat colon mucosa. The product of the reaction is the 2,4-dienone, 13-oxooctadecadienoic acid. Enzyme activity was determined by HPLC analysis of incubation mixtures as well as by measuring the increase in absorbance at 285 nm, which represents formation of the 2,4-dienone chromophore. Characteristics of the reaction with respect to protein concentration, time of incubation and substrate dependence were investigated. Several inhibitors of known dehydrogenases had no effect on the 13-HODE dehydrogenase. These include, ethanol, indomethacin, 6-methyl-17-Hydroxyprogesterone Acetate, 4-(diethylamino)-benzaldehyde, and aspirin. The enzyme was mildly inhibited by pyrazole, 4-methylpyrazole and ibuprofen. Disulfiram was found to be a potent inhibitor of enzyme activity with an IC50 of 200 microM. Inhibitor specificity, and other characteristics of the reaction suggest the enzyme is neither alcohol dehydrogenase, diol dehydrogenase, nor a prostaglandin dehydrogenase. It is possible this enzyme plays an important role in the response of the colonic mucosa to the mitogenic effect of oxidized fatty acids.

David L. Winner – One of the best experts on this subject based on the ideXlab platform.

  • Metabolism of oxidized linoleic acid: characterization of 13-hydroxyoctadecadienoic acid dehydrogenase activity from rat colonic tissue.
    Biochimica et biophysica acta, 1991
    Co-Authors: Sonja M. Earles, Joel C. Bronstein, David L. Winner, Arthur W. Bull
    Abstract:

    An oxidized derivative of linoleic acid, 13-hydroxyoctadecadienoic acid (13-HODE), is dehydrogenated by an NAD+ dependent dehydrogenase present in rat colon mucosa. The product of the reaction is the 2,4-dienone, 13-oxooctadecadienoic acid. Enzyme activity was determined by HPLC analysis of incubation mixtures as well as by measuring the increase in absorbance at 285 nm, which represents formation of the 2,4-dienone chromophore. Characteristics of the reaction with respect to protein concentration, time of incubation and substrate dependence were investigated. Several inhibitors of known dehydrogenases had no effect on the 13-HODE dehydrogenase. These include, ethanol, indomethacin, 6-methyl-17-Hydroxyprogesterone Acetate, 4-(diethylamino)-benzaldehyde, and aspirin. The enzyme was mildly inhibited by pyrazole, 4-methylpyrazole and ibuprofen. Disulfiram was found to be a potent inhibitor of enzyme activity with an IC50 of 200 microM. Inhibitor specificity, and other characteristics of the reaction suggest the enzyme is neither alcohol dehydrogenase, diol dehydrogenase, nor a prostaglandin dehydrogenase. It is possible this enzyme plays an important role in the response of the colonic mucosa to the mitogenic effect of oxidized fatty acids.

Joel C. Bronstein – One of the best experts on this subject based on the ideXlab platform.

  • Metabolism of oxidized linoleic acid: characterization of 13-hydroxyoctadecadienoic acid dehydrogenase activity from rat colonic tissue.
    Biochimica et biophysica acta, 1991
    Co-Authors: Sonja M. Earles, Joel C. Bronstein, David L. Winner, Arthur W. Bull
    Abstract:

    An oxidized derivative of linoleic acid, 13-hydroxyoctadecadienoic acid (13-HODE), is dehydrogenated by an NAD+ dependent dehydrogenase present in rat colon mucosa. The product of the reaction is the 2,4-dienone, 13-oxooctadecadienoic acid. Enzyme activity was determined by HPLC analysis of incubation mixtures as well as by measuring the increase in absorbance at 285 nm, which represents formation of the 2,4-dienone chromophore. Characteristics of the reaction with respect to protein concentration, time of incubation and substrate dependence were investigated. Several inhibitors of known dehydrogenases had no effect on the 13-HODE dehydrogenase. These include, ethanol, indomethacin, 6-methyl-17-Hydroxyprogesterone Acetate, 4-(diethylamino)-benzaldehyde, and aspirin. The enzyme was mildly inhibited by pyrazole, 4-methylpyrazole and ibuprofen. Disulfiram was found to be a potent inhibitor of enzyme activity with an IC50 of 200 microM. Inhibitor specificity, and other characteristics of the reaction suggest the enzyme is neither alcohol dehydrogenase, diol dehydrogenase, nor a prostaglandin dehydrogenase. It is possible this enzyme plays an important role in the response of the colonic mucosa to the mitogenic effect of oxidized fatty acids.

H. P. G. Schneider – One of the best experts on this subject based on the ideXlab platform.