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Tamm-Horsfall urinary glycoprotein. The subunit structure.

A P Fletcher, A Neuberger, W A Ratcliffe

    The Biochemical Journal
    |November 1, 1970
    PubMed
    Summary

    Tamm-Horsfall glycoprotein

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    Area of Science:

    • Biochemistry
    • Glycoprotein characterization

    Background:

    • Tamm-Horsfall glycoprotein is a major urinary protein.
    • Its molecular weight and structure are not fully elucidated.

    Purpose of the Study:

    • To determine the subunit molecular weight of Tamm-Horsfall glycoprotein.
    • To investigate the structural integrity of Tamm-Horsfall glycoprotein.

    Main Methods:

    • Gel filtration chromatography (Sephadex G-200) in sodium dodecyl sulfate.
    • Disc gel electrophoresis in sodium dodecyl sulfate.
    • N-terminal amino acid analysis after cyanogen bromide cleavage.
    • Ultracentrifugation in sodium dodecyl sulfate and formic acid.
    • Disulfide bond reduction.

    Main Results:

    • Subunit molecular weights ranging from 76,000-82,000 were determined by gel filtration and electrophoresis.
    • N-terminal analysis yielded a minimum molecular weight of 79,000 ± 6,000.
    • Ultracentrifugation showed sedimentation as a single component.
    • Disulfide bond reduction did not alter subunit molecular weight, suggesting intrachain linkages.

    Conclusions:

    • Tamm-Horsfall glycoprotein has a subunit molecular weight of approximately 79,000.
    • Disulfide bonds are intrachain, contributing to structural stability.

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