Open AccessAffinity Labeling of the Heavy and Light Chains of a Myeloma Protein with Anti-2,4-Dinitrophenyl Activity
Author(s) -
Joseph Haimovich,
David Givol,
Herman N. Eisen
Publication year - 1970
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.67.4.1656
Subject(s) - dinitrophenyl , lysine , ethylenediamine , covalent bond , chemistry , immunoglobulin light chain , derivative (finance) , stereochemistry , biochemistry , amino acid , organic chemistry , biology , antibody , economics , financial economics , immunology
A mouse myeloma protein with high affinity for 2,4-dinitrophenyl (Dnp) ligands was reacted with the bromoacetyl derivatives ofN -Dnp-ethylenediamine andε -N -Dnp-L-lysine. Up to 1.4 sites per protein molecule were covalently labeled. The labeling reactions were essentially completely blocked by a large excess of Dnp ligands that do not combine covalently (e.g.,ε -Dnp-L-lysine). Analyses of the labeled protein revealed that the bromoacetyl derivative ofN -Dnp-ethylenediamine reacted exclusively with tyrosyl in the light chain, while the derivative ofε -Dnp-L-lysine reacted exclusively with lysyl in the heavy chain. The findings support the conclusion that chains are involved in forming specific combining sites.