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Iduronate sulfatase from human placenta.

P Di Natale, A Daniele

    Biochimica Et Biophysica Acta
    |May 8, 1985
    PubMed
    Summary
    This summary is machine-generated.

    Researchers purified the iduronate sulfatase enzyme from human placenta, determining its molecular weight. This enzyme is likely composed of a single polypeptide chain, aiding in understanding its structure and function.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Human Placental Biology

    Background:

    • Iduronate sulfatase is a crucial enzyme.
    • Understanding its properties is important for biochemical research.

    Purpose of the Study:

    • To purify the major enzyme component of iduronate sulfatase from human placenta.
    • To determine the molecular weight and subunit composition of the purified enzyme.

    Main Methods:

    • Multi-step purification procedure.
    • Sucrose gradient centrifugation for native enzyme molecular weight estimation.
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions.

    Main Results:

    • Achieved a 30,000-fold purification of iduronate sulfatase.

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  • Native enzyme molecular weight estimated at 80,000 +/- 10,000 Da.
  • SDS-PAGE revealed a single protein band with a molecular weight of 82,000 Da under reducing conditions.

    • Conclusions:

    • The major enzyme component of human placental iduronate sulfatase is likely a single polypeptide chain.
    • The estimated molecular weight of this polypeptide chain is between 80,000 and 90,000 Da.