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- W2022086781 abstract "The induced optical activity (circular dichroism) originating from the interaction of dinitrophenylated and trinitrophenylated haptens with antibody has been used as a probe of the antibody combining site. A mouse IgA myeloma protein (MOPC-315) with high affinity for DNP- and TNP-ligands was employed as an example of a homogeneous antibody. The sign and the magnitude of circular dichroism bands differed when DNP- and TNP-haptens were bound, respectively, to the single homogeneous MOPC-315 protein. Differences in the relative magnitude of distinct circular dichroism bands also were seen when the DNP-group was incorporated into different haptens and complexed with the same homogeneous antibody. The circular dichroism spectra of hapten complexed with native MOPC-315 protein, mildly reduced and alkylated protein, and reassociated MOPC-315 protein were similar. The induced circular dichroism of ϵ-DNP-lysine bound to a goat anti-DNP antibody differed markedly from the circular dichroism spectrum of the same ligand bound to the MOPC-315 protein. Circular dichroism has been shown to offer a new and powerful parameter for studying and comparing the fine structure of the combining sites of antibodies of similar specificity, and to probe the reformed site resulting from the reassociation of heavy and light polypeptide chains." @default.
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- W2022086781 date "1971-09-01" @default.
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- W2022086781 title "Induced optical activity (circular dichroism) of antibody-hapten complexes" @default.
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- W2022086781 doi "https://doi.org/10.1016/0022-1759(71)90006-8" @default.
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