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Estrogen sulfotransferase in human placenta.

L Tseng, L Y Lee, J Mazella

    Journal of Steroid Biochemistry
    |May 1, 1985
    PubMed
    Summary

    Human placental estrogen sulfotransferase (ESFT) was purified, revealing its isoelectric point and binding properties. Kinetic studies confirmed estradiol as the preferred substrate for this key sulfotransferase enzyme.

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Estrogen sulfotransferase (ESFT) plays a crucial role in steroid hormone metabolism.
    • Understanding the properties of human placental ESFT is important for comprehending estrogen regulation.

    Purpose of the Study:

    • To partially purify and characterize human placental estrogen sulfotransferase (ESFT).
    • To investigate the substrate specificity of the purified enzyme.

    Main Methods:

    • Partial purification of ESFT from term placental cytosol using (NH4)2SO4 precipitation and agarose gel chromatography.
    • Isoelectric focusing and chromatofocusing were employed to assess enzyme properties.
    • Affinity chromatography using an estradiol-conjugated resin was utilized for purification and characterization.
    • SDS-polyacrylamide gel electrophoresis (SDS-PAGE) determined the molecular weight of the enzyme.

    Main Results:

    • Partially purified ESFT exhibited an isoelectric point (pI) of 5.8, consistent with bovine adrenal ESFT.
    • The enzyme bound to an estradiol affinity resin but was difficult to elute.
    • SDS-PAGE revealed a major protein band at 68,000 daltons.
    • Kinetic studies indicated that estradiol (E2) is the preferred substrate, with relative sulfurylation rates of 1 for E2, 0.3 for estrone, and 0.08 for estriol and dehydroepiandrosterone at 4 μM.

    Conclusions:

    • Human placental ESFT was successfully partially purified and characterized.
    • The enzyme demonstrates a strong preference for estradiol as a substrate.
    • The findings provide insights into the biochemical properties and substrate specificity of human placental estrogen sulfotransferase.

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