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Large scale isolation of functionally active components of the human complement system.

C H Hammer, G H Wirtz, L Renfer

    The Journal of Biological Chemistry
    |April 25, 1981
    PubMed
    Summary
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    This study presents an efficient method for isolating multiple human complement components with high purity and activity. The developed scheme allows for large-scale purification of these vital proteins for research and diagnostic applications.

    Area of Science:

    • Immunology
    • Biochemistry
    • Proteomics

    Background:

    • The human complement system is crucial for innate immunity.
    • Isolation of functional complement components is essential for research and diagnostics.
    • Existing purification methods often yield low quantities or reduced activity.

    Purpose of the Study:

    • To develop a scalable and efficient purification scheme for multiple human complement components.
    • To obtain complement proteins in a functionally pure state with high hemolytic activity.
    • To provide a reliable source of purified complement factors for various applications.

    Main Methods:

    • Utilized a multi-step chromatographic approach, primarily DEAE-Sephacel, for component separation.
    • Incorporated pre-treatment steps including protease inhibition and plasminogen depletion.

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  • Employed polyethylene glycol fractionation and ultrafiltration for initial plasma processing.

    • Main Results:

    • Achieved high recovery of milligram to gram quantities of complement components from large plasma volumes.
    • Several components, including C3, C5, C7, C9, and C1EI, were isolated with high purity and full hemolytic activity.
    • Demonstrated significant purification folds for key components like C3 (up to 64-fold) and C9 (up to 297-fold) after the first chromatographic step.

    Conclusions:

    • The presented scheme offers an effective and scalable method for purifying human complement components.
    • The isolated components are suitable for use as reagents due to their high purity and preserved activity.
    • This purification strategy facilitates further research into complement biology and its clinical implications.