Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Multiple complexes of thrombin and heparin.

J R Evington, P A Feldman, M Luscombe

    Biochimica Et Biophysica Acta
    |May 12, 1986
    PubMed
    Summary
    This summary is machine-generated.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Development and characterization of the high-purity factor IX, Replenine.

    Haemophilia : the official journal of the World Federation of Hemophilia·2016
    Same author

    The A245K mutation exposes another stage of the bacterial L-lactate dehydrogenase reaction mechanism.

    Biochemistry·2001
    Same author

    A scintillation proximity assay for rna detection.

    Analytical biochemistry·2001
    Same author

    Need for diagnostic screening of Herpes simplex virus in patients with nongonococcal urethritis.

    Clinical infectious diseases : an official publication of the Infectious Diseases Society of America·2000
    Same author

    Production of an activated form of Bacillus stearothermophilus L-2-hydroxyacid dehydrogenase by directed evolution.

    Protein engineering·2000
    Same author

    A general method for relieving substrate inhibition in lactate dehydrogenases.

    Protein engineering·1999

    Heparin

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Pharmacology

    Background:

    • Thrombin and heparin interactions are crucial in blood coagulation.
    • Heparin's role in catalyzing thrombin-antithrombin complex formation is well-established.
    • Understanding these molecular dynamics is key to anticoagulant therapies.

    Purpose of the Study:

    • To investigate the stoichiometry and binding characteristics of thrombin-heparin complexes.
    • To elucidate the influence of heparin molecular weight on thrombin-antithrombin complex formation.
    • To determine the dissociation constants of these interactions.

    Main Methods:

    • Fluorescence polarization assays were employed.
    • Titration experiments were conducted at varying ionic strengths.

    Related Experiment Videos

  • Dissociation constants were estimated by reversing titration.

    • Main Results:

    • Two distinct thrombin-heparin complexes (complex 1 and complex 2) were identified.
    • Complex 1 stoichiometry varied with heparin molecular weight, while complex 2 was consistently 1:1.
    • Dissociation constants for complex 2 and the thrombin-heparin-antithrombin complex were found to be independent of heparin size.
    • Increased heparin size lowered the Km for the heparin-catalyzed thrombin-antithrombin reaction.

    Conclusions:

    • Heparin molecular weight influences the initial formation of thrombin-heparin complexes.
    • The binding affinity of thrombin to heparin and the subsequent antithrombin complex is largely independent of heparin size.
    • Heparin acts as a scaffold, potentially facilitating rapid thrombin transfer to antithrombin in a size-dependent manner.