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Related Experiment Videos

Fluorescein in human plasma in vitro

H Lund-Andersen, B Krogsaa

    Acta Ophthalmologica
    |October 1, 1982
    PubMed
    Summary

    This study details a new method for measuring fluorescein in human plasma. Ultrafiltration separates protein-bound and free fluorescein, revealing limited protein binding capacity.

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    Area of Science:

    • Biochemistry
    • Analytical Chemistry
    • Pharmacokinetics

    Background:

    • Fluorescein is a widely used fluorescent dye.
    • Understanding its behavior in biological fluids like plasma is crucial for accurate quantification.
    • Plasma protein binding influences drug distribution and efficacy.

    Purpose of the Study:

    • To develop and describe a method for determining fluorescein concentration in human plasma.
    • To investigate the binding characteristics of fluorescein to plasma proteins.
    • To quantify both protein-bound and free fractions of fluorescein.

    Main Methods:

    • Utilized ultrafiltration to separate fluorescein bound to plasma proteins from free fluorescein.
    • Quantitated both the bound and free fractions of fluorescein.
    • Assessed the reversibility and sensitivity of protein binding to pH, temperature, and gas tensions.

    Main Results:

    • Fluorescein exhibits reversible binding to plasma proteins.
    • Protein binding is largely unaffected by physiological variations in pH, temperature, and gas tensions.
    • At total plasma concentrations of 10⁻⁶ to 10⁻⁴ g/mL, approximately 15% of fluorescein was free.
    • At a total concentration of 10⁻³ g/mL, 45% of fluorescein was free, indicating saturation of binding sites.

    Conclusions:

    • The described ultrafiltration method effectively quantifies fluorescein fractions in human plasma.
    • Fluorescein protein binding is a significant factor, but with limited capacity.
    • These findings are important for pharmacokinetic studies and clinical applications of fluorescein.

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