Work

Affinity Labeling of the Heavy and Light Chains of a Myeloma Protein with Anti-2,4-Dinitrophenyl Activity

Year: 1970

Type: article

Abstract: A mouse myeloma protein with high affinity for 2,4-dinitrophenyl (Dnp) ligands was reacted with the bromoacetyl derivatives of N-Dnp-ethylenediamine and (epsilon)-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., (epsilon)-Dnp-L-lysine). Analyses of the labeled protein revealed that the bromoacetyl derivative of N-Dnp-ethylenediamine reacted exclusively with tyrosyl in the light chain, while the derivative of (epsilon)-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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.67.4.1656

Authors: Joseph Haimovich, David Givol, Herman N. Eisen

Institutions: Weizmann Institute of Science, Washington University in St. Louis

Language: English

Topic: Monoclonal and Polyclonal Antibodies Research

Subfield: Radiology, Nuclear Medicine and Imaging

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: U.S. Department of Defense, World Health Organization

OpenAlex ID: W2016867156