Open AccessA simpler sort of antibody.
Author(s) -
Linda Masat,
Matthias Wabl,
Judith P. Johnson
Publication year - 1994
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.91.3.893
Subject(s) - immunoglobulin light chain , monomer , monoclonal antibody , kappa , antibody , microbiology and biotechnology , chemistry , size exclusion chromatography , cell fusion , antigen , biology , biochemistry , cell , genetics , polymer , philosophy , enzyme , linguistics , organic chemistry
The monoclonal antibody NEMO is directed against a molecule expressed by human cells of the melanocytic lineage. Although obtained by conventional immunization and fusion procedures, NEMO consists solely of kappa light chain. SDS/PAGE analysis indicates that the kappa chains are present as both monomers and dimers. When these two forms were separated by gel filtration, only the monomeric form bound antigen. As kappa light chains from the myeloma MOPC-41 and the hybridoma MORK do not bind to the melanocytic cells, we conclude that the binding specificity of NEMO resides in the variable region.