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Fluorescence color converter

The fluorescence color converter technique [32] can, in principle, overcome much of this power loss by replacing the white light emitter with a blue-emitting organic stack, and the absorbing filters with green and red fluorescent dyes. Thus when a green pixel is desired, the OLED underneath is turned on and the blui... [Pg.240]

Donor and acceptor levels are the active centers in most phosphors, as in zinc sulfide [1314-98-3] ZnS, containing an activator such as Cu and various co-activators. Phosphors are coated onto the inside of fluorescent lamps to convert the intense ultraviolet and blue from the mercury emissions into lower energy light to provide a color balance closer to daylight as in Figure 11. Phosphors can also be stimulated directly by electricity as in the Destriau effect in electroluminescent panels and by an electron beam as in the cathodoluminescence used in television and cathode ray display tubes and in (usually blue) vacuum-fluorescence alphanumeric displays. [Pg.421]

The course of the reaction has not been fully clarified. Hydrolytic and aromatization processes are probably responsible for the formation of colored or fluorescent deriva4 tives (cf. Potassium Hydroxide Reagent). For instance, sevin is converted to a-naphthalkali metal salt of the o-hydroxycinnamic acid pro- duced by hydrolytic cleavage of the pyrone ring is converted from the non-fluorescent cis- to the fluorescent trans-form by the action of long-wavelength UV light (X = 365 nm) [2]. [Pg.202]

Direct and indirect competition formats, illustrated in Figure 1, are widely used for both qualitative and quantitative immunoassays. Direct competition immunoassays employ wells, tubes, beads, or membranes (supports) on to which antibodies have been coated and in which proteins such as bovine semm albumin, fish gelatin, or powdered milk have blocked nonspecific binding sites. Solutions containing analyte (test solution) and an analyte-enzyme conjugate are added, and the analyte and antibody are allowed to compete for the antibody binding sites. The system is washed, and enzyme substrates that are converted to a chromophore or fluorophore by the enzyme-tracer complex are added. Subsequent color or fluorescence development is inversely proportionate to the analyte concentration in the test solution. For this assay format, the proper orientation of the coated antibody is important, and anti-host IgG or protein A or protein G has been utilized to orient the antibody. Immunoassays developed for commercial purposes generally employ direct competition formats because of their simplicity and short assay times. The price for simplicity and short assay time is more complex development needed for a satisfactory incorporation of the label into the antibody or analyte without loss of sensitivity. [Pg.681]

Fig. 21 Fluorescein-based chemodosimeter molecules for ROS. Whereas faintly colored and weakly fluorescent 54 reacts rather nonspecifically to green and highly fluorescent 55 (a hROS = highly reactive oxygen species), colorless and nonfluorescent 56 is selectively converted into green and highly fluorescent 57 in the presence of H2O2... Fig. 21 Fluorescein-based chemodosimeter molecules for ROS. Whereas faintly colored and weakly fluorescent 54 reacts rather nonspecifically to green and highly fluorescent 55 (a hROS = highly reactive oxygen species), colorless and nonfluorescent 56 is selectively converted into green and highly fluorescent 57 in the presence of H2O2...
In 1937 Arnow showed that tyrosine could be converted into DOPA by ultraviolet radiation51 and that the DOPA produced in this manner was subsequently destroyed by further irradiation, the solutions becoming red-brown in color (presumably due to the formation of dopachrome).51 In 1939 Konzett and Weis reported that the blood pressure-raising effect of adrenaline solutions was lost on ultraviolet irradiation and that the solutions became colored and fluorescent the initial red color fades to reddish yellow.62 This phenomenon suggests the initial formation of adrenochrome, followed by its isomerization to adrenolutin, both of these compounds being virtually void of pressor activity. Similarly to the radiation-induced hydroxylation of tyrosine mentioned above, synephrine was first... [Pg.212]

The enzyme attached to antibody 2 is critical for quantitative analysis. Figure 19-14 shows two ways in which the enzyme can be used. The enzyme can transform a colorless reactant into a colored product. Because one enzyme molecule catalyzes the same reaction many times, many molecules of colored product are created for each analyte molecule. The enzyme thereby amplifies the signal in the chemical analysis. The higher the concentration of analyte in the original unknown, the more enzyme is bound and the greater the extent of the enzyme-catalyzed reaction. Alternatively, the enzyme can convert a nonfluorescent reactant into a fluorescent product. Colorimetric and fluorometric enzyme-linked immunosorbent assays are sensitive to less than a nanogram of analyte. Pregnancy tests are based on the immunoassay of a placental protein in urine. [Pg.412]

ELISA can be used to quantify the amount of a specific protein antigen in a sample. The antibody is bound to an inert polymer support, then exposed to the sample. Unbound protein is washed away and a second antibody that reacts with the antigen at a different epitope is added. The second antibody used is one that has an enzyme attached to it that converts a colorless or nonfluorescent substrate into a colored or fluorescent product. The amount of second antibody bound, and hence the amount of protein antigen present in the original sample, is determined by quantification of the intensity of color or fluorescence produced. [Pg.112]


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