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Antibody-antigen recognition kinetics

Determining the thermodynamics and kinetics of recognition between biomolecules, particularly when one of the two is immobilized on a substrate, is of considerable current interest, as for example, antibody-antigen recognition, recognition of single-stranded DNA oligonucleotides by partially or totally complementary DNA strands, and many other possible analytical applications. [Pg.325]

Specific, rapid, and high-affinity recognition of antigens by antibodies is essential for the host s immune system to respond to invasion by foreign cells and pathogens. Pecht and Lancet have presented a cogent analysis of antibody interactions with haptens, and the interested reader will find their examination of the kinetics and thermodynamics to be particularly lucid. Briefly, for the simple one-step binding scheme. [Pg.61]

The non-covalent interactions in many of natural compounds commonly referred as biomolecules are responsible for veiy important biological processes. The molecular recognition process in biological systems is observed between such species as receptor-ligand, antigen-antibody, sugar-lectin, DNA-protein, RNA-ribosome and others. The kinetics of the majority of glycan-protein interactions is fast and with dissociation... [Pg.434]


See other pages where Antibody-antigen recognition kinetics is mentioned: [Pg.5989]    [Pg.610]    [Pg.325]    [Pg.335]    [Pg.216]    [Pg.201]    [Pg.28]    [Pg.41]    [Pg.240]    [Pg.315]    [Pg.503]    [Pg.252]    [Pg.93]    [Pg.84]    [Pg.66]    [Pg.448]    [Pg.50]    [Pg.223]    [Pg.34]    [Pg.223]    [Pg.140]    [Pg.5986]    [Pg.5990]    [Pg.1046]    [Pg.2]   
See also in sourсe #XX -- [ Pg.325 , Pg.326 , Pg.327 , Pg.328 , Pg.329 , Pg.330 ]




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Antibody-antigen

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Antigens antigen recognition

Kinetic recognition

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