High impact information on Fluorescence Polarization

• Patients receiving transplants after January 2002 (n=89) were prospectively monitored by C2 levels (target: 1,500+/-200 ng/mL [fluorescence-polarization immunoassay]) [1].
• The effect of the binding of fructose-6-P or MgATP2- on the polarization fluorescence of the emission of Trp88 in Pfk-2 indicates changes in the local mobility of the Trp88 in both enzyme complexes [2].
• After 4 days of treatment, membranes and their liposomes prepared from treated animals possessed a greater fluidity than did their control (diluent, 0.9% NaCl) counterparts, as assessed by steady-state fluorescence-polarization techniques using several different fluorophores [3].
• A study of the interaction between bovine cardiac-muscle cyclic AMP-dependent protein kinase and cyclic AMP using fluorescence-polarization spectroscopy [4].
• The high nonspecific binding of verapamil to the liposomes had no detectable effect on the fluidity of their membrane, as seen in fluorescence-anisotropy studies with the fluorescent probe DPH [5].

Associations of Fluorescence Polarization with chemical compounds

• The stability of reconstituted enzyme is strongly influenced by the presence of CoA ligands as shown by fluorescence-polarization measurements [6].
• Close proximity of the two Trp residues (less than 1 nm) is suggested from steady-state and time-resolved fluorescence-anisotropy measurements in vitrified medium [95% (by mass) glycerol at -38 degrees C] [7].
• Blood samples were collected for a 26-hour period, and serum concentrations of cyclosporine were measured using fluorescence-polarization immunoassay technology [8].
• The effects of the neurotoxin MPTP (1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine) and its toxic metabolites MPDP+ (1-methyl-4-phenyl-2,3-dihydropyridinium) and MPP+ (1-methyl-4-phenylpyridinium) on liposomal membrane were assessed using fluorescence-polarization and carboxyfluorescein leakage studies as well as in biological membrane preparations [9].
• The apoenzyme is stable for a long period of time when kept in 50% ethylene glycol at -18 degrees C. Steady-state fluorescence-polarization measurements of protein-bound FAD indicate that reconstituted lipoamide dehydrogenase possesses a high stability which is governed by the low dissociation rate constant of the apoenzyme-FAD complex [6].

Gene context of Fluorescence Polarization

• Fluorescence-polarization changes in mononuclear blood leucocytes after PHA incubation: differences in cells from patients with and without neoplasia [10].
• This interaction is specific for non-native domains since native alpha-lactalbumin fails to interact with Hip. Fluorescence-anisotropy measurements indicate that reduced, carboxymethylated lactalbumin binds Hip with a Kd of 5 microM [11].
• From the analysis of inhibition and from fluorescence-polarization data it follows that for an efficient binding of these alkaloids to glutamate dehydrogenase the presence of coenzyme is necessary [12].
• To study the interaction between eIF4E and cap, and to identify small molecule inhibitors of their binding, we synthesized a fluorescent-labeled cap analogue and used it to develop a fluorescence-polarization assay [13].
• In this study, polarization fluorescence is used to demonstrate that complexes of alpha 2-macroglobulin with trypsin fluorescence is used to demonstrate that complexes of alpha 2-macroglobulin with trypsin can digest beta-endorphin, adrenocorticotropin, and beta-lipotropin [14].

Analytical, diagnostic and therapeutic context of Fluorescence Polarization

• Predictions of free (unbound) serum phenytoin concentration by three methods were compared with results obtained by the Abbott TDx Free Phenytoin ultrafiltration and fluorescence-polarization immunoassay technique [15].

References