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Related Experiment Videos

The complete amino acid sequence of human complement factor H.

J Ripoche1, A J Day, T J Harris

  • 1Department of Biochemistry, University of Oxford, U.K.

The Biochemical Journal
|January 15, 1988
PubMed
Summary
This summary is machine-generated.

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Researchers sequenced human factor H (complement system protein) and found 1213 amino acids in 20 repeating units. This protein sequence reveals potential alternative splicing and allelic variants, crucial for understanding complement regulation.

Area of Science:

  • Molecular Biology
  • Immunology
  • Protein Chemistry

Background:

  • Factor H is a key regulatory protein within the human complement system.
  • Understanding its complete amino acid sequence is vital for elucidating complement pathway function and dysregulation.
  • Previous knowledge of factor H structure was incomplete.

Purpose of the Study:

  • To determine the complete amino acid sequence of human factor H.
  • To investigate the structural organization and potential variations of factor H.
  • To explore mechanisms underlying factor H expression, such as alternative splicing.

Main Methods:

  • Sequencing of three overlapping complementary DNA (cDNA) clones encoding human factor H.
  • Bioinformatic analysis to derive the amino acid sequence and identify structural features.

Related Experiment Videos

  • Comparison of deduced sequence with isolated factor H protein.

    • Main Results:

    • The complete amino acid sequence of human factor H comprises 1213 residues, including an 18-residue leader sequence.
    • Factor H is organized into 20 homologous repeat units, each approximately 60 amino acids long, sharing homology with other complement proteins.
    • A tyrosine/histidine polymorphism was identified, suggesting allelic variation, and two C-terminal residues deduced from cDNA are absent in plasma-derived factor H.
    • Evidence for alternative splicing indicates at least two factor H mRNA species.

    Conclusions:

    • The deduced amino acid sequence provides a comprehensive structural basis for human factor H.
    • The identified polymorphism and variations suggest genetic heterogeneity in factor H.
    • Alternative splicing likely contributes to the diversity of factor H functional forms.