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Radio-ligand binding

The riboflavin binding protein that occurs in eggs has been exploited for the radio-ligand binding assay of riboflavin. Because binding to the protein quenches the native fluorescence of riboflavin, it can be exploited for a direct titrimetric fluorescence assay of the vitamin in urine and other biological samples (Kodentsova et al., 1995). [Pg.178]

Furchgott RF. Pharmacological characterization of receptors its relation to radio-ligand-binding studies. FedProc 1978 37 115-120. [Pg.102]

Kll. Korenman, S. G., Radio-ligand binding assay of specific estrogens using a soluble uterine macromolecule. J. Clin. Endocrinol. 28, 127-130 (1968). [Pg.135]

Optimization of molecularly imprinted polymers for radio-ligand binding assays... [Pg.79]

Mayes, A. Lowe, C.R. Optimization of molecularly imprinted polymers for radio-ligand binding assays. Royal Society of Chemistry Cambridge, UK, 1998 Vol. 25, 28-36. Andersson, L.I. Muller, R. Vlatakis, G. Mosbach, K. Mimics of the binding sites of opioid receptors obtained by molecular imprinting of enkephalin and morphine. Proc. Natl. Acad. Sci. USA 1995, 92, 4788 792. [Pg.390]


See other pages where Radio-ligand binding is mentioned: [Pg.877]    [Pg.100]    [Pg.103]    [Pg.51]    [Pg.758]    [Pg.40]    [Pg.41]    [Pg.49]    [Pg.19]    [Pg.20]    [Pg.186]    [Pg.681]    [Pg.194]    [Pg.199]    [Pg.151]   
See also in sourсe #XX -- [ Pg.20 ]




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