Monoclonal IgM antibody exhibiting high-affinity binding and cryoglobulin properties.

D. W. Ballard, D. M. Kranz, E. W. Voss

Research output: Contribution to journalArticlepeer-review


A monoclonal IgM antibody (18-2-3) derived from cell fusion of (NZB X NZW) F1 splenocytes following secondary immunization with fluorescein-conjugated keyhole limpet hemocyanin was shown to exhibit high intrinsic binding affinity and cryoinsolubility. Affinity-purified preparations were determined to be IgM by immunochemical, electrophoretic, and chromatographic analyses. An intrinsic association constant (Ka) of 2.9 X 10(10) M-1 (at 2 degrees C) was measured by first-order dissociation-rate analysis. Antibody solubility at low concentration (approximately equal to 50 micrograms/ml) was shown, by absorption spectroscopy, to be temperature dependent between 4 degrees C and 32 degrees C. Insolubility at low temperature (4 degrees C) was reversible in the presence of homologous fluorescyl hapten, indicative of active site involvement in the mechanism of cryoglobulin-18-2-3 complex formation. Characteristics of clone 18-2-3 are discussed in terms of (i) its potential use as a model for examining the mechanism of cryoprecipitation and (ii) the proposed relationship between affinity maturation and the IgM to IgG class switch.

Original languageEnglish (US)
Pages (from-to)5071-5074
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number16
StatePublished - Aug 1983
Externally publishedYes

ASJC Scopus subject areas

  • General


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