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. 1970 Dec;67(4):1656–1661. doi: 10.1073/pnas.67.4.1656

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

Joseph Haimovich †, David Givol ‡, Herman N Eisen §
PMCID: PMC283408  PMID: 4099105

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 ε-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 of N-Dnp-ethylenediamine reacted exclusively with tyrosyl in the light chain, while the derivative of ε-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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