Abstract
The extent to which unlabeled ligand competes with radioactive ligand for a limited number of receptor sites in a macromolecule serves as a basis for quantitation in competitive protein binding assays. Often, picogram amounts of a particular compound can be estimated. Once the receptor molecule and labeled ligand are available, the assays are relatively simple to perform: mixtures containing labeled ligand, receptor molecule, and sample are incubated; free labeled ligand is separated from receptor-bound labeled ligand, and the extent of binding is determined. Although natural receptors have been employed in several competitive binding assays, their use is limited by their availability and stability. Thus antibodies have been produced to develop radioimmunoassays.
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