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Purification and structural studies on the complement-system control protein beta 1H (Factor H).

R B Sim, R G DiScipio

    The Biochemical Journal
    |August 1, 1982
    PubMed
    Summary
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    Researchers developed an efficient method to isolate human beta 1H (Factor H) protein. This crucial complement system regulator was characterized, and its cofactor activity was confirmed in a two-chain form.

    Area of Science:

    • Biochemistry
    • Immunology
    • Proteomics

    Background:

    • The complement system is a vital part of innate immunity.
    • Beta 1H (Factor H) protein regulates complement activation.
    • Efficient isolation and characterization of Factor H are crucial for understanding its function.

    Purpose of the Study:

    • To develop an efficient isolation procedure for human beta 1H (Factor H) from plasma.
    • To characterize the chemical composition and physical properties of Factor H.
    • To investigate the functional activity of Factor H fragments.

    Main Methods:

    • Plasma protein isolation techniques.
    • Biochemical analysis of protein composition and structure.
    • N-terminal amino acid sequencing.

    Related Experiment Videos

  • Proteolytic cleavage studies using trypsin.
  • Cofactor activity assays for C3b-inactivator.

    • Main Results:

    • An efficient isolation method for beta 1H (Factor H) was established.
    • Factor H is a 155,000 mol.wt. glycoprotein with 9.3% carbohydrate content.
    • Proteolytic cleavage yields a two-chain form retaining full C3b-inactivator cofactor activity.
    • N-terminal sequence of 17 amino acids was determined.
    • Proteolytic fragments were compared to related cofactor proteins.

    Conclusions:

    • The developed isolation procedure is effective for obtaining human Factor H.
    • Factor H's functional cofactor activity is preserved in its two-chain cleaved form.
    • Understanding Factor H structure-function relationships is important for complement system regulation.