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Related Experiment Videos

Third component of human complement: purification from plasma and physicochemical characterization

B D Tack, J W Prahl

    Biochemistry
    |October 5, 1976
    PubMed
    Summary
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    This study details the purification of the third complement component (C3) from human plasma. Researchers achieved high purity and characterized its molecular weight and N-terminal sequences, confirming its two-chain structure.

    Area of Science:

    • Biochemistry
    • Immunology
    • Proteomics

    Background:

    • The third component of complement (C3) is crucial for the immune system's complement cascade.
    • Understanding C3 structure and properties is vital for immunological research.

    Purpose of the Study:

    • To purify and characterize the third component of complement (C3) from human plasma.
    • To determine the molecular weight, N-terminal sequence, and homogeneity of purified C3.

    Main Methods:

    • Purification involved poly(ethylene glycol) fractionation, plasminogen depletion, affinity chromatography, ion-exchange chromatography, gel filtration, and hydroxylapatite adsorption.
    • Homogeneity was assessed by immunological criteria and SDS-PAGE.
    • Molecular weight was determined by sedimentation equilibrium.

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  • N-terminal sequencing was performed using automated Edman degradation.

    • Main Results:

    • Purified C3 exhibited apparent homogeneity with 33% protein and 31% hemolytic activity recovery.
    • Partial specific volume was 0.736 mlgm-1.
    • Weight average molecular weight was 187,650 +/- 5650.
    • Automated Edman degradation revealed a double N-terminal sequence (Ser-Val), consistent with a two-chain structure.

    Conclusions:

    • The study successfully purified and characterized human C3.
    • The findings confirm the two-chain structure of C3 and provide key physical and chemical properties.