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

Comparative aspects of prothrombin activation.

D A Walz

    Bibliotheca Haematologica
    |January 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Researchers studied prothrombin activation in humans, chickens, and cows. They found evolutionary evidence suggesting gene duplication occurred before bird and mammal divergence.

    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

    A hierarchy of disulfide-bonded subunits: the quaternary structure of Eudistylia chlorocruorin.

    Biochemistry·1998
    Same author

    Electrospray ionization mass spectrometric study of the multiple intracellular monomeric and polymeric hemoglobins of Glycera dibranchiata.

    Journal of protein chemistry·1998
    Same author

    Expression of thrombospondin 1 on the surface of activated platelets mediates their interaction with the heavy chains of human kininogens through Lys 244-Pro 254.

    Thrombosis and haemostasis·1998
    Same author

    Molecular symmetry of the dodecamer subunit of Lumbricus terrestris hemoglobin.

    Journal of molecular biology·1996
    Same author

    Electron spin resonance and fluorescence studies of the conformational environment of the thiol groups of thrombospondin: interactions with thrombin.

    Biochemistry·1995
    Same author

    Solid tumor cells express functional "tethered ligand" thrombin receptor.

    Cancer research·1995
    Same journal

    Incorporation of allosteric effectors of hemoglobin in red blood cells. Physiological effects.

    Bibliotheca haematologica·1985
    Same journal

    Resealed red blood cells as a new blood transfusion product.

    Bibliotheca haematologica·1985
    Same journal

    Entrapment of L-asparaginase in red blood cells. A strategy to improve treatment of acute lymphoblastic leukemia.

    Bibliotheca haematologica·1985
    Same journal

    G6PD encapsulation and metabolic properties of loaded erythrocytes.

    Bibliotheca haematologica·1985
    Same journal

    Entrapment of normal and mutant glucose 6-phosphate dehydrogenase (G6PD) within G6PD deficient erythrocytes.

    Bibliotheca haematologica·1985
    Same journal

    Encapsulation and pharmacokinetics of drugs in bovine and canine carrier erythrocytes.

    Bibliotheca haematologica·1985
    See all related articles

    Area of Science:

    • Biochemistry
    • Evolutionary Biology
    • Hematology

    Background:

    • Prothrombin is a key vitamin K-dependent protein in the blood coagulation cascade.
    • Understanding prothrombin activation provides insights into hemostasis and related disorders.

    Purpose of the Study:

    • To investigate and compare the activation pathways of purified prothrombin from human, bovine, and chicken species.
    • To analyze the structural similarities and differences in prothrombin fragments and thrombin chains across these species.
    • To infer evolutionary relationships based on conserved protein sequences and structures.

    Main Methods:

    • Purification of prothrombin from human, bovine, and chicken plasma.
    • Analysis of prothrombin activation products, including fragments and thrombin chains.

    Related Experiment Videos

  • Amino acid sequence comparison of vitamin K-dependent regions and internal homology domains.

    • Main Results:

    • Chicken prothrombin activation yields fragments similar to bovine, with distinct thrombin chain sizes.
    • Human thrombin shows a shorter A chain compared to chicken and bovine thrombin.
    • High sequence similarity in vitamin K-dependent regions (33/46 residues identical) across all three species.
    • Internal homology regions observed in human and bovine fragments are also present in chicken fragments.

    Conclusions:

    • The structural organization and activation of prothrombin are conserved across mammals and birds.
    • Evidence suggests a partial gene duplication event in prothrombin evolution predates the divergence of birds and mammals over 300 million years ago.
    • Comparative analysis of prothrombin activation aids in understanding the evolution of coagulation factors.