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

Antigenic mapping of a human lambda light chain: correlation with three dimensional structure.

J J Marchalonis1, F Dedeoglu, H Kaymaz

  • 1University of Arizona, College of Medicine, Tucson 85724.

Journal of Protein Chemistry
|April 1, 1992
PubMed
Summary

This study maps antigenic markers on human immunoglobulin lambda light chains using synthetic peptides. Key determinants are located in linear N- and C-terminal segments, with some conformational dependence in other regions.

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

Gathering expert consensus to inform a proposed trial in chronic nonbacterial osteomyelitis (CNO).

Clinical immunology (Orlando, Fla.)·2023
Same author

Probing the boundaries of the extended immunoglobulin family of recognition molecules: jumping domains, convergence and minigenes.

Immunology today·2014
Same author

Further comments on the molecular members of extended immunoglobulin family.

Immunology today·2014
Same author

The T-cell antigen receptor: the minimal hypothesis revisited.

Immunology today·2014
Same author

Immunomodulation by immunopeptides and autoantibodies in aging, autoimmunity, and infection.

Annals of the New York Academy of Sciences·2006
Same author

A recognition of Joseph R. Goodman's scientific contributions.

Cellular and molecular biology (Noisy-le-Grand, France)·2005

Area of Science:

  • Immunology
  • Protein Chemistry
  • Structural Biology

Background:

  • The three-dimensional structure and amino acid sequence of human immunoglobulin light chains are known.
  • However, the precise locations of antigenic markers specific to lambda chains remain undetermined.

Purpose of the Study:

  • To map the antigenic determinants of the human lambda light chain Mcg.
  • To identify regions contributing to antigenicity and assess the role of conformational factors.

Main Methods:

  • Utilized a comprehensive set of synthetic overlapping peptides representing the complete sequence of the lambda chain Mcg.
  • Tested peptide binding with rabbit and goat antisera specific for lambda chain determinants.
  • Analyzed peptide contributions to antigenic reactivity and conformational antigenicity.

Related Experiment Videos

Main Results:

  • Identified specific antigenic determinants in both the constant and variable domains (first and third framework) of the lambda chain.
  • The fourth framework of the variable region, encoded by the joining gene, showed cross-reactivity with T cell receptor beta chains.
  • Major determinants were localized to linear N- and C-terminal segments, lacking significant conformational folding.
  • Antigenic segments in the V region (residues 78-93) and C region (residues 177-192) demonstrated strong conformational dependence.

Conclusions:

  • Specific antigenic determinants of lambda light chains are distributed across multiple domains.
  • Linear segments are primary sites for major determinants, while other regions rely on conformation for antigenicity.
  • The findings provide a detailed map of lambda chain antigenic sites, with implications for antibody structure-function studies.