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

A new fluorogenic substrate for plasmin.

P A Pierzchala, C P Dorn, M Zimmerman

    The Biochemical Journal
    |December 1, 1979
    PubMed
    Summary
    This summary is machine-generated.

    A novel fluorogenic substrate enables a simple and sensitive assay for plasmin (an enzyme crucial in blood clot breakdown). This method accurately quantifies plasmin, even with interfering substances present.

    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

    Search for Extremely-High-Energy Neutrinos and First Constraints on the Ultrahigh-Energy Cosmic-Ray Proton Fraction with IceCube.

    Physical review letters·2025
    Same author

    Measurement of Atmospheric Neutrino Oscillation Parameters Using Convolutional Neural Networks with 9.3 Years of Data in IceCube DeepCore.

    Physical review letters·2025
    Same author

    Search for an eV-Scale Sterile Neutrino Using Improved High-Energy ν_{μ} Event Reconstruction in IceCube.

    Physical review letters·2024
    Same author

    Observation of Seven Astrophysical Tau Neutrino Candidates with IceCube.

    Physical review letters·2024
    Same author

    Baseline levels of circulating galectin-1 associated with radiographic hand but not radiographic knee osteoarthritis at a two-year follow-up.

    Osteoarthritis and cartilage open·2024
    Same author

    PDGFRβ promotes oncogenic progression via STAT3/STAT5 hyperactivation in anaplastic large cell lymphoma.

    Molecular cancer·2022

    Area of Science:

    • Biochemistry
    • Enzymology
    • Analytical Chemistry

    Background:

    • Plasmin is a key enzyme in fibrinolysis, essential for regulating blood clot breakdown.
    • Accurate and sensitive assays for plasmin are vital for clinical diagnostics and research.
    • Existing methods may lack specificity or sensitivity in complex biological samples.

    Purpose of the Study:

    • To develop and validate a new fluorogenic peptide substrate for the direct and sensitive assay of plasmin activity.
    • To establish an assay method that is linear over a wide range of enzyme concentrations.
    • To demonstrate the specificity of the assay in the presence of other proteases and biological fluids.

    Main Methods:

    • Synthesis of a novel fluorogenic peptide substrate: 7-(N-succinoylalanylphenylalanyl-lysylamido)-4-methylcoumarin trifluoroacetate salt.

    Related Experiment Videos

  • Development of a simple and direct assay for plasmin using the synthesized substrate.
  • Characterization of assay linearity and sensitivity.
  • Assessment of plasmin specificity using the inhibitor Trasylol and kinetic constant differences, in the presence of thrombin and HeLa cell culture fluids.

    • Main Results:

    • The new substrate allows for a simple and direct assay of plasmin.
    • Assay results demonstrate linearity across a broad spectrum of plasmin concentrations.
    • The assay is highly sensitive, detecting as little as 10(-5) CTA units of plasmin.
    • Specific quantification of plasmin is achievable even in the presence of thrombin and in HeLa cell culture fluids, by utilizing Trasylol and kinetic differences.

    Conclusions:

    • The developed fluorogenic peptide substrate provides a robust tool for sensitive and specific plasmin quantification.
    • This assay method offers advantages in simplicity, linearity, and specificity, making it suitable for various research and potential diagnostic applications.
    • The assay's ability to perform in complex biological matrices enhances its utility in studying plasmin activity in physiological and pathological conditions.