Abstract
In the past several years affinity labeling has emerged as a powerful method for studying ligand-receptor interactions. The logic of an affinity labeling experiment (Singer, 1967) is described in Eq. (1)–(3). A reactive group, X (electrophilic or photolabile), is attached to the natural ligand, L. If the resulting modified ligand ĹX retains high affinity for the native ligand receptor site and forms a non-covalent complex, R.ĹX, [Eq. (1)], then, at low ĹX concentration, covalent attachment via the reaction in Eq. (2), a first order process, will proceed at a much faster rate than attachment via the reaction in Eq. (3), a second order process, and specific attachment to the ligand site will be achieved.
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Cooperman, B.S. (1976). Photoaffinity Labeling of Proteins and More Complex Receptors. In: Smith, K.C. (eds) Aging, Carcinogenesis, and Radiation Biology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1662-7_17
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