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The Journal of Immunology, 1971, 107: 12-18.
Copyright © 1971 by The American Association of Immunologists, Inc.
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Comparative Ligand-Binding by Purified Nurse Shark Natural Antibodies and Anti-2,4-Dinitrophenyl Antibodies from Other Species1

Edward W. Voss, Jr.2, Stuart Rudikoff3 and M. M. Sigel4

Department of Microbiology, University of Illinois, Urbana, Illinois, The National Cancer Institute, Bethesda, Maryland and the Department of Microbiology, University of Miami School of Medicine, Miami, Florida

Abstract

A population of 19S IgM specific for the 2,4-dinitrophenyl group was purified from normal nurse shark sera by immune precipitation with high concentrations of dinitrophenylated protein antigens. Hapten-binding properties of the purified antibody were difficult to measure in equilibrium dialysis because of the apparent low affinity of the antibody combining sites. Fluorescence quenching and spectral shift studies revealed significant binding with the bis-{alpha}, {varepsilon}-DNP-l-lysine ligand but not with mono-{varepsilon}-DNP-l-lysine. Comparative binding studies with these two ligands in the fluorescence quenching assay indicated that the combining sites of purified natural shark antibody resembled low-affinity, antigen-induced antibody in shark and other species. Qmax determinations and fluorometric titrations with antibody subunits indicated that binding of bis-{alpha}, {varepsilon}-DNP-l-lysine was specific for the antibody combining sites.

Footnotes

1 This investigation was supported by United States Public Health Service Research Grants AI-05758 and AI-08288 from the National Institute of Allergy and Infectious Diseases.

2 Department of Microbiology, University of Illinois, Urbana, Illinois.

3 National Cancer Institute, Bethesda, Maryland.

4 Department of Microbiology, University of Miami School of Medicine, Miami, Florida.






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