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. Author manuscript; available in PMC: 2014 Jan 1.

Published in final edited form as: Biochem J. 2013 Jan 1;449(1):91–99. doi: 10.1042/BJ20121088

A) Binding curves for monovalent DNP/IgE^DNP (■), monovalent DNP-Pro/IgE^DNP (), and monovalent dansyl/IgE^dansyl (□) interactions are shown. Binding was observed by monitoring the fluorescence quenching of tryptophan. Values for the binding constants are K_d^DNP = 22 ± 2 nM, K_d^DNP-Pro = 550 ± 40 nM and K_d^dansyl = 54 ± 4 nM. Control experiments done with DNP/IgE^dansyl, DNP-Pro/IgE^dansyl, or dansyl/IgE^DNP did not show any cross-reactivity, Figure S1. Data represents means ± SD of triplicate experiments. B) DLS data demonstrates the aggregation of IgE^DNP and IgE^dansyl in response to addition of a stoichiometric concentration of HtTA. The size of the monomeric IgE antibodies was 7.5 nm and increased to 16 nm upon the addition of the HtTA.

Inline graphic — A) Binding curves for monovalent DNP/IgE^DNP (■), monovalent DNP-Pro/IgE^DNP (), and monovalent dansyl/IgE^dansyl (□) interactions are shown. Binding was observed by monitoring the fluorescence quenching of tryptophan. Values for the binding constants are K_d^DNP = 22 ± 2 nM, K_d^DNP-Pro = 550 ± 40 nM and K_d^dansyl = 54 ± 4 nM. Control experiments done with DNP/IgE^dansyl, DNP-Pro/IgE^dansyl, or dansyl/IgE^DNP did not show any cross-reactivity, Figure S1. Data represents means ± SD of triplicate experiments. B) DLS data demonstrates the aggregation of IgE^DNP and IgE^dansyl in response to addition of a stoichiometric concentration of HtTA. The size of the monomeric IgE antibodies was 7.5 nm and increased to 16 nm upon the addition of the HtTA.