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Related Experiment Videos

Trypsin activation of human factor XI

C Mannhalter, S Schiffman, A Jacobs

    The Journal of Biological Chemistry
    |April 10, 1980
    PubMed
    Summary

    Human factor XI activation by trypsin yields three distinct protein chains, not two as previously reported. This finding clarifies the molecular processing of factor XI during blood coagulation.

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    Area of Science:

    • Biochemistry
    • Hematology
    • Molecular Biology

    Background:

    • Human factor XI is a zymogen with two ~80,000 Mr chains.
    • Activation by trypsin or clotting factors involves proteolytic cleavage.
    • Previous reports suggested cleavage to 48,000 and 33,000 Mr chains.

    Purpose of the Study:

    • To reinvestigate the molecular details of trypsin activation of human factor XI.
    • To clarify the chain composition of trypsin-activated factor XI.

    Main Methods:

    • Proteolytic cleavage analysis of factor XI using trypsin.
    • SDS-PAGE to determine molecular weights (Mr) of resulting chains.
    • Kinetic studies to elucidate the cleavage pathway.

    Main Results:

    • Trypsin-activated factor XI was found to contain three chains with apparent Mr of 46,000, 37,000, and 26,000.
    • Kinetic analysis indicated the initial cleavage of the 80,000 Mr chain into 46,000 and 37,000 Mr chains.
    • A subsequent cleavage, likely of the 46,000 Mr chain, produced the 26,000 Mr chain.

    Conclusions:

    • The trypsin activation of human factor XI results in a three-chain structure.
    • The previously proposed two-chain model is inaccurate.
    • This revised understanding impacts the study of factor XI function in coagulation.

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