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Related Experiment Videos

Third component of complement (C3): structural properties in relation to functions.

V A Bokisch, M P Dierich, H J Mūller-Eberhard

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1975
    PubMed
    Summary
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    The third component of complement (C3) has alpha and beta chains. Upon activation, C3 fragments bind to cell membranes, playing a key role in the complement system

    Area of Science:

    • Immunology
    • Biochemistry

    Background:

    • The third component of complement (C3) is central to complement system function.
    • Understanding C3's structure and fragmentation is crucial for immunology.

    Purpose of the Study:

    • Investigate topological relationships of C3 polypeptide chains, fragments, and functional sites.
    • Elucidate the mechanisms of C3 activation and fragment binding.

    Main Methods:

    • Analysis of C3 polypeptide chains (alpha and beta) and their molecular weights.
    • Enzymatic cleavage studies to identify C3 fragments (C3a, C3b, C3c, C3d).
    • Investigation of binding affinities of C3 fragments to biological membranes and cell receptors.

    Main Results:

    • C3 comprises alpha (120,000 Da) and beta (75,000 Da) chains linked by disulfide and noncovalent bonds.

    Related Experiment Videos

  • C3 activation by C3 convertase cleaves the alpha-chain, releasing C3a and forming C3b.
  • C3b binds membranes via the C3d portion; C3c and C3d bind specific cell receptors.

    • Conclusions:

    • All physiologically occurring C3 fragments (C3a, C3b, C3c, C3d) originate from alpha-chain enzymatic cleavage.
    • C3b and C3d fragments mediate interactions with cell surfaces through specific receptors.
    • The study clarifies the structural basis for C3 function in the complement cascade.