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Photoaffinity Labeling of Proteins and More Complex Receptors

  • Barry S. Cooperman

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.

Keywords

Label Pattern Noncovalent Complex Diazo Compound Photoaffinity Label Covalent Bond Formation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1976

Authors and Affiliations

  • Barry S. Cooperman
    • 1
  1. 1.Department of ChemistryUniversity of PennsylvaniaPhiladelphiaUSA

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