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 kringle-specific monoclonal antibody

W R Church1, T L Messier, L A Ouellette

  • 1Department of Biochemistry, College of Medicine, University of Vermont, Burlington 05405.

Hybridoma
|October 1, 1994
PubMed
Summary

A novel antibody targets a conserved antigenic determinant in kringle domains of plasma proteins like prothrombin and plasminogen. This finding reveals structural similarities in lysine-binding sites across key blood proteins.

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

The humoral response to human factor VIII in hemophilia A mice.

Journal of thrombosis and haemostasis : JTH·2006
Same author

Mecamylamine effects on haloperidol-induced catalepsy and defecation.

The International journal of neuroscience·2001
Same author

Antithrombotic efficacy of a novel murine antihuman factor IX antibody in rats.

Arteriosclerosis, thrombosis, and vascular biology·1999
Same author

The ras-related GTPase rac1 regulates a proliferative pathway selectively utilized by G-protein coupled receptors.

Oncogene·1998
Same author

A serotonin receptor gene (5HT1A) variant found in a Tourette's syndrome patient.

Biochemical and biophysical research communications·1996
Same author

Factor X Stockton: a mild bleeding diathesis associated with an active site mutation in factor X.

Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis·1996

Area of Science:

  • Biochemistry
  • Immunology
  • Proteomics

Background:

  • Kringle domains are crucial structural motifs in plasma proteins involved in blood coagulation and fibrinolysis.
  • These domains contain lysine-binding sites essential for protein function.

Purpose of the Study:

  • To generate and characterize a monoclonal antibody (alpha HII-5) against a conserved epitope in prothrombin kringle 2.
  • To investigate the presence of homologous antigenic determinants in other kringle-containing plasma proteins.

Main Methods:

  • Production of a murine monoclonal antibody (alpha HII-5) against a synthetic peptide from human prothrombin kringle 2.
  • Immunoassays (solution-phase and solid-phase) and immunoblotting to assess antibody binding specificity.

Main Results:

  • Antibody alpha HII-5 bound prothrombin and miniplasminogen in solution but recognized prothrombin, plasminogen, recombinant tissue plasminogen activator (tPA), and apo(a) on solid surfaces.
  • Immunoblotting confirmed binding to determinants on prothrombin fragment 2 and plasminogen kringle 5.

Conclusions:

  • A conserved antigenic determinant exists within the lysine-binding site region of certain kringle domains, notably in prothrombin kringle 2 and plasminogen kringle 5.
  • This determinant is accessible on plasminogen only under specific conditions, such as surface adsorption or removal of other kringle domains.

Related Experiment Videos