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Related Experiment Videos

An albumin dimer in urine.

J P Beilby, C Chin, P Garcia-Webb

    Clinical Chemistry
    |March 1, 1985
    PubMed
    Summary

    Albumin dimers were found in urine but not serum of a patient with liver and kidney failure. This dimerization, via disulfide bonds, reduced thyroxine binding and was unstable during storage.

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    Area of Science:

    • Biochemistry
    • Nephrology
    • Hepatology

    Background:

    • Alcoholic liver disease and chronic renal failure can alter protein structure and function.
    • Serum albumin is a key transport protein with known binding capacities.

    Observation:

    • Aged albumin dimer (approx. 134,000 Da) was detected in freshly voided urine.
    • Monomeric albumin was also present in urine, but absent in serum.
    • The patient was a 53-year-old male with alcoholic liver disease and chronic renal failure.

    Findings:

    • Albumin dimerization occurred via disulfide bonds, distinct from previously reported sites.
    • The albumin dimer exhibited reduced [125I]thyroxine-binding capacity compared to monomeric albumin.
    • The dimer proved unstable across all tested storage temperatures.

    Implications:

    • Disulfide-mediated albumin dimerization in urine may indicate renal dysfunction.
    • Altered thyroxine binding by urinary albumin dimers could have diagnostic or prognostic significance.
    • The instability of the dimer suggests rapid post-excretion modifications or inherent structural lability.

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