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Characterization of human complement components C6 and C7

R G Discipio, J Gagnon

    Molecular Immunology
    |November 1, 1982
    PubMed
    Summary
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    Researchers purified and characterized human complement components C6 and C7. These plasma proteins, C6 and C7, were found to be distinct single-chain proteins with different molecular weights and amino terminal residues, showing no sequence homology.

    Area of Science:

    • Immunology
    • Protein Chemistry

    Background:

    • The human complement system is crucial for innate immunity.
    • Understanding individual complement components is vital for elucidating system function.

    Purpose of the Study:

    • To purify and characterize human complement components C6 and C7.
    • To determine the biochemical properties and potential relationship between C6 and C7.

    Main Methods:

    • Protein purification techniques were employed for C6 and C7 isolation.
    • Molecular weight determination was performed.
    • Amino-terminal residue analysis was conducted.
    • Primary sequence analysis was utilized to assess homology.

    Main Results:

    • Human complement component C6 was purified as a single-chain plasma protein (104,800 Da) with 3.8% carbohydrate and alanine at the N-terminus.

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  • Human complement component C7 was purified as a single-chain plasma protein (92,400 Da) with 6.4% carbohydrate and serine at the N-terminus.
  • Primary sequence analysis revealed no evidence of homology between C6 and C7.
  • Conclusions:

    • Human complement components C6 and C7 are distinct proteins.
    • Biochemical characterization provides foundational data for further functional studies of C6 and C7.
    • The lack of homology suggests divergent evolutionary paths or specialized roles within the complement cascade.