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Characterization of a cDNA coding for human factor X.

S P Leytus, D W Chung, W Kisiel

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1984
    PubMed
    Summary
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    Researchers identified the complete amino acid sequence for human factor X, a key protein in blood coagulation. This discovery provides crucial insights into the molecular mechanisms of the coagulation cascade.

    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Hematology

    Background:

    • Human factor X is a critical plasma protein involved in the blood coagulation cascade.
    • Understanding its structure is essential for comprehending hemostasis and related disorders.

    Purpose of the Study:

    • To determine the complete amino acid sequence of human factor X.
    • To elucidate the synthesis and processing of factor X.

    Main Methods:

    • Screening of a human liver cDNA library using an antibody to human factor X.
    • Sequencing of the largest cDNA insert.
    • Deduction of amino acid sequence from cDNA.

    Main Results:

    • Identified a cDNA insert of 1137 base pairs coding for human factor X.

    Related Experiment Videos

  • Determined the complete amino acid sequence, including light and heavy chains, connecting region, and polyadenylation signals.
  • Factor X is synthesized as a single-chain polypeptide and processed into mature chains.

    • Conclusions:

    • The complete amino acid sequence of mature human factor X has been established.
    • The deduced sequence shows homology to other vitamin K-dependent serine proteases, suggesting conserved functional domains.
    • This provides a foundation for further research into factor X function and therapeutic strategies.