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Immunoreactive granulocyte elastase in human serum

K Ohlsson, A S Olsson

    Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
    |November 1, 1978
    PubMed
    Summary
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    A new radioimmunoassay accurately measures human granulocyte elastase in blood. This method overcomes challenges with tracer binding, revealing active elastase is rapidly inhibited in serum.

    Area of Science:

    • Biochemistry
    • Immunology
    • Clinical Chemistry

    Background:

    • Human granulocyte elastase (HGE) is a key protease involved in inflammatory processes.
    • Accurate measurement of HGE in biological samples is crucial for understanding its role in disease.
    • Existing assays faced challenges with tracer instability and non-specific binding.

    Purpose of the Study:

    • To develop and validate a specific radioimmunoassay for quantifying human granulocyte elastase in blood.
    • To address and overcome technical limitations in previous HGE measurement methods.

    Main Methods:

    • Development of a radioimmunoassay using diisopropylfluorophosphate-inactivated, radioiodinated HGE tracer.
    • Optimization of reaction conditions, including increased NaCl concentration, to minimize non-specific binding.

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  • Sephadex G-100 gel filtration to analyze HGE distribution in normal human serum.

    • Main Results:

    • The developed radioimmunoassay effectively measures HGE in blood.
    • Increased NaCl concentration successfully prevented non-specific binding of the tracer to serum proteins and Sephadex.
    • Normal human serum contains approximately 135 µg/L of HGE, primarily bound to alpha1-antitrypsin.

    Conclusions:

    • The optimized radioimmunoassay provides a reliable method for HGE determination.
    • The findings suggest HGE is released in an active form from cells and immediately complexed by alpha1-antitrypsin in serum.