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- W1269275112 abstract "Publisher Summary The chemical structure of the combining site of antibodies was a central paradox in immunology: How could an apparently infinite range of combining specificities reside in what appeared to be a very monotonous group of proteins, closely related in their structure? Considered from this viewpoint, it is interesting that, relative to other proteins with combining sites, for example, enzymes, antibodies are a late evolutionary acquisition, present only in vertebrates, and their synthesis is confined to only one type of cell: the lymphocyte. It has therefore been a long-standing question whether the structure of the antibody site is based on principles that differ from those governing the structure of the active sites of other proteins. This chapter explains the theory of affinity labeling, criteria of affinity labeling, choosing the labeling reagent, affinity-labeled residues at the combining site of antibodies, the labeled chain, position of affinity labeled residues. It also discusses the synthesis of reagents, antibodies and affinity labeling of antibodies." @default.
- W1269275112 created "2016-06-24" @default.
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- W1269275112 date "1977-01-01" @default.
- W1269275112 modified "2023-10-05" @default.
- W1269275112 title "[53] Affinity labeling of antibody combining sites as illustrated by anti-dinitrophenyl antibodies" @default.
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- W1269275112 doi "https://doi.org/10.1016/s0076-6879(77)46057-9" @default.
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