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

[Interrelation between thrombin structure and its stability].

M V Kolodzeĭskaia, G L Volkov

    Ukrains'Kyi Biokhimichnyi Zhurnal (1999 )
    |March 29, 2006
    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

    [Thrombin and anticoagulant therapy].

    Ukrains'kyi biokhimichnyi zhurnal (1999 )·2009
    Same author

    Role of A-chain in functioning of the active site of human alpha-thrombin.

    Biochemistry. Biokhimiia·2008
    Same author

    [Sodium ions as the effector of catalytic action of alpha-thrombin].

    Ukrains'kyi biokhimichnyi zhurnal (1999 )·2007
    Same author

    [Human thrombin: drug stability and stabilization].

    Ukrains'kyi biokhimichnyi zhurnal (1999 )·2007
    Same author

    Immobilization of mouse single-chain antibodies for affinity chromatography using the cellulose-binding protein.

    Ukrains'kyi biokhimichnyi zhurnal (1999 )·2007
    Same author

    [Technology of immunoglobulin production. I. Technological aspects of purification].

    Ukrains'kyi biokhimichnyi zhurnal (1999 )·2006

    Amino acids protect human thrombin from heat inactivation, with L-arginine and DL-lysine showing the strongest stabilizing effects. This stabilization likely involves amino acids binding to thrombin's reactive center, enhancing enzyme stability.

    Area of Science:

    • Biochemistry
    • Enzymology

    Context:

    • Human thrombin is a crucial enzyme in coagulation.
    • Understanding enzyme stabilization mechanisms is vital for therapeutic applications.
    • Temperature inactivation poses a challenge for enzyme stability.

    Purpose:

    • To investigate the mechanism of human thrombin stabilization by various amino acids.
    • To determine the effect of amino acids on thrombin's thermal stability at optimal pH.
    • To correlate amino acid stabilizing effects with thrombin specificity.

    Summary:

    • Most amino acids offer partial protection against thermal inactivation of human thrombin.
    • L-arginine and DL-lysine exhibited the most significant stabilizing effects.
    • Stabilization is linked to amino acid binding at the enzyme's reactive center, similar to enzyme-substrate interactions, and may inhibit autolysis.

    Related Experiment Videos

    Impact:

    • Reveals a novel mechanism for enhancing thrombin stability using amino acids.
    • Suggests potential strategies for developing more stable thrombin-based therapeutics.
    • Provides insights into enzyme structure-function relationships and active site dynamics.