Affinity labeling of the antibody combining site

Antibodies and myeloma proteins against haptens comprise the most commonly used experimental system in which the determination of the antibody structure-function relationship has been attempted. Affinity labeling studies of antibodies were initiated by Singer, Wofsy and Metzger using diazonium labeling reagents attached to a benzene arsonate hapten. Converse and Richards used diazoketones attached to dinitrophenyl (DNP) haptens as affinity labels, while Givol, Wilchek and coworkers used bromoacetyl derivatives attached to DNP haptens to label DNP-specific antibodies and MOPC 315 (a myeloma protein that binds DNP). A homologous series of reagents was prepared in which the bromoacetyl group was attached to the DNP hapten at progressively increasing distances from the haptenic moiety, thus allowing the labeling of residues in the combining site at various distances from the DNP ring. A photoaffinity label using aromatic azides was introduced by Porter's group. The photoaffinity reagent was introduced to overcome the limitations of the other reagents which can interact only with electrophilic reagents; the azide reacts with any amino acid residue. In addition, the design of this reagent made the chemical reactive group (L) part of the hapten.

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