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Related Experiment Videos

Quantitation of complement factor D in human serum by a solid-phase radioimmunoassay.

S R Barnum, M A Niemann, J F Kearney

    Journal of Immunological Methods
    |March 16, 1984
    PubMed
    Summary

    A new radioimmunoassay accurately measures human D levels. This protein D is stable in normal, acute-phase, and lupus sera but is lost upon heat inactivation.

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    Area of Science:

    • Immunology
    • Biochemistry

    Background:

    • Human protein D is a component of serum.
    • Understanding protein D's behavior in different physiological states and its stability is crucial.

    Purpose of the Study:

    • To develop a sensitive assay for quantifying human protein D.
    • To investigate the concentration of protein D in various human serum types.
    • To determine the stability of protein D during complement activation and heat inactivation.

    Main Methods:

    • Development of a sensitive solid-phase radioimmunoassay for human protein D.
    • Measurement of protein D concentrations in normal, acute-phase, and systemic lupus erythematosus sera.
    • In vitro testing of serum decomplementation via classical and alternative complement pathways.

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  • Assessment of protein D stability after heat inactivation of serum.

    • Main Results:

    • The radioimmunoassay quantifies human protein D with a sensitivity of 1-2 ng/ml.
    • Comparable mean concentrations of protein D were observed in normal (1.8 µg/ml), acute-phase (2.3 µg/ml), and lupus sera (2.5 µg/ml).
    • Protein D levels were not significantly depleted by activation of the classical or alternative complement pathways.
    • Heat inactivation of serum at 56°C for 30 minutes resulted in a near-complete loss of antigenic protein D.

    Conclusions:

    • A reliable method for quantifying human protein D has been established.
    • Protein D levels remain consistent across normal, acute-phase, and systemic lupus erythematosus conditions.
    • Protein D is resistant to complement-mediated activation but is susceptible to heat denaturation.