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

Phenotypic similarity between T-cell antigen binding molecules.

R E Cone1, A Takeda, K D Beaman

  • 1Department of Pathology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Conn.

Experimental and Clinical Immunogenetics
|January 1, 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

Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer disease.

Journal of neuropathology and experimental neurology·2000
Same author

Response of feline intradental nerve fibers to tooth cutting by Er:YAG laser.

Lasers in surgery and medicine·2000
Same author

[Care of diabetic patients. 2. The importance of patient education].

Nihon Naika Gakkai zasshi. The Journal of the Japanese Society of Internal Medicine·2000
Same author

Clinical benefits of steroid therapy on surgical stress in patients with esophageal cancer.

Surgery·2000
Same author

Serum p53 antibody is a useful tumor marker in superficial esophageal squamous cell carcinoma.

Cancer·2000
Same author

Impact of circulating p53 autoantibody monitoring after endoscopic resection in mucosal gastric cancer.

Endoscopy·2000
Same journal

Nomenclature and overview of the mouse (Mus musculus and Mus sp.) immunoglobulin kappa (IGK) genes.

Experimental and clinical immunogenetics·2002
Same journal

Nomenclature of the human immunoglobulin lambda (IGL) genes.

Experimental and clinical immunogenetics·2002
Same journal

Oligonucleotide fishing for STAT6: cross-talk between IL-4 and chemokines.

Experimental and clinical immunogenetics·2002
Same journal

Use of human recombinant DNase I expressed in COS-7 cells as an immunogen to produce a specific anti-DNase I antibody.

Experimental and clinical immunogenetics·2002
Same journal

In situ activated intestinal T cells expanded in vitro--without addition of antigen--produce IFN-gamma and IL-10 and preserve their function during growth.

Experimental and clinical immunogenetics·2002
Same journal

Increased frequency of the C3*F allele and the Leiden mutation of coagulation factor V in patients with severe coronary heart disease who survived myocardial infarction.

Experimental and clinical immunogenetics·2002
See all related articles

Researchers purified T-cell antigen binding molecules (TABM) and analyzed their peptide maps. Findings suggest structural similarities and distinctions, indicating variable and constant domains in these crucial immune molecules.

Area of Science:

  • Immunology
  • Molecular Biology
  • Protein Chemistry

Background:

  • T-cell antigen binding molecules (TABM) play a critical role in adaptive immunity.
  • Understanding the structural characteristics of TABM is essential for deciphering immune recognition mechanisms.

Purpose of the Study:

  • To purify and structurally characterize T-cell antigen binding molecules (TABM) specific for various antigens.
  • To investigate the potential presence of variable and constant domains within TABM.

Main Methods:

  • Purification of TABM using affinity chromatography and monoclonal antibody adsorption.
  • In vitro synthesis of TABM via translation of immunopurified mRNA.
  • Radiolabeling (125I) of purified TABM and T-cell membrane proteins.
  • Proteolytic digestion using Staphylococcus V8 protease.

Related Experiment Videos

  • Two-dimensional (2D) gel peptide mapping for peptide resolution.
  • Amino acid analysis of specific TABM.
  • Main Results:

    • Peptide maps revealed similarities and distinctions among TABM specific for different antigens (TNP, oxazalone, azobenzenearsonate, sheep erythrocytes).
    • Structural comparisons of peptide maps and amino acid analyses provided evidence for conserved and variable regions.
    • These findings suggest the existence of distinct variable and constant domains within TABM.

    Conclusions:

    • The structural analysis supports the hypothesis of variable and constant domains in T-cell antigen binding molecules.
    • This domain structure is likely fundamental to the diverse antigen recognition and immune signaling functions of T-cells.