Hapten-induced enhancement of monoclonal antibody binding in ELISA.

We have recently reported [Hall T. J., Stenzel-Poore M. and Rittenburg M. B., Sixth International Congress of Immunology, Toronto. Abstract 2.15.27, p. 108 (1986)] on the fine specificity analysis of six monoclonal antibodies (MAbs) which utilize lambda 1 (lambda 1) light chains, produced from BALB/c mice immunized with PC-KLH. Binding of these MAbs to PC-histone in ELISA was inhibited by the PC analogue nitrophenylphosphocholine (NPPC) but not by PC itself, thus distinguishing these group II antibodies from the group I PC binding myeloma proteins such as TEPC 15 and MOPC 603 [Leon and Young, (1971) Biochemistry 10, 1424-1429]. Three of these lambda MAbs showed a reproducible 2-4 fold increase in binding in ELISA at certain concns (10-100 microM) of NPPC and one of them (PCG2b-3) was chosen to examine this observation further.