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- W54470086 abstract "ABSTRACT The specificity and affinity exhibited by the binding sites of antibodies is a result of the interactions of a particular spatial combination of certain residues within the site with the complementary counterpart groups of the hapten. The dynamic equilibrium between hapten and antibody has been shown to involve a single step: Ab + Hk12/k21 AbH In order to probe the dimensions of the antibody combining site and to determine the nature and localization of the attracting forces, a correlation between structure of a series of systematically varied ligands and their specific rates of binding (k12) and dissociation (k21) to a certain binding site is carried out using the chemical relaxation T-jump method to determine these rates. The combining site of the homogeneous murine IgA protein 315 which has affinity to polynitrophenyl derivatives has been probed using over 40 different ligands. The results enabled the construction of a proposed model for the site; four subsites of interaction are observed: (a) The polynitrophenyl binding subsite, (b) two hydrophobic subsites, and (c) an electrostatic (positive) subsitg. The overall minimal dimensions of this site are 12 × 6A. Another homogeneous site which is at present being studied is that of the phosphoryl choline binding protein HOPC 8. Normally induced, heterogeneous antibodies binding oligoalanine peptides have also been investigated by this kinetic method. Specific rates were determined for the interaction of haptens of different lengths with different eluates of the antibody population. Using fluorescent probes, covalently attached to the hapten (oligoalanines or DNP) the depth of the combining site has been examined. This has been accomplished by measurements of the circular and linear polarized components of the bound ligands carrying the fluorophores." @default.
- W54470086 created "2016-06-24" @default.
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- W54470086 date "1974-01-01" @default.
- W54470086 modified "2023-09-24" @default.
- W54470086 title "KINETIC MAPPING OF ANTIBODY BINDING SITES" @default.
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- W54470086 doi "https://doi.org/10.1016/b978-0-12-637150-5.50010-9" @default.
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