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Extrinsic Cotton Effects Characteristic of Specific Hapten-Antibody Interactions
Michael Glaser and S. J. Singer
Proceedings of the National Academy of Sciences of the United States of America
Vol. 68, No. 10 (Oct., 1971), pp. 2477-2479
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/61071
Page Count: 3
You can always find the topics here!Topics: Antibodies, Haptens, Cotton, Active sites, Binding sites, Wavelengths, Biochemistry, Titration, Myeloma proteins, Absorption spectra
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The reversible binding of the haptens 2,4-dinitrophenyllysine (DNP-lysine) and 2,4,6-trinitrophenyllysine (TNP-lysine) to either the nitrophenyl-binding myeloma protein MOPC-315 or to pooled mouse anti-DNP or anti-TNP antibodies produces large and characteristic extrinsic Cotton effects (in the circular dichroic spectra). Despite the similarities in binding characteristics of the three proteins, the circular dichroic spectra produced by the haptens bound to the active sites of these proteins were markedly different. Extrinsic Cotton effects, therefore, provide a powerful new probe of the structure of the reversible complex formed between a hapten and an antibody active site.
Proceedings of the National Academy of Sciences of the United States of America © 1971 National Academy of Sciences