Dye phenol red

Serum albumin circulates in the blood stream transporting essential nutrients such as fatty acids to peripheral tissue. Transported molecules, called ligands, often have a special affinity for selected binding sites on proteins and nucleic acids. In this experiment, the dynamics of ligand-protein interactions will be explored with the binding of the dye phenol red to bovine serum albumin. The technique of gel filtration will be used to separate the dye-protein complex. Data will be analyzed in order to construct binding curves. 

Extensive research on albumin has led to an increasingly clear picture of ligand binding. The dye phenol red has been widely used as a model for the binding of natural ligands to proteins. Experimental results have shown that each molecule of albumin binds at least six molecules of phenol red. The presence of fatty acids such as decanoate, palmitate, stearate, and oleate... 

In this experiment, you will evaluate the binding of the dye phenol red to bovine serum albumin. Increasing amounts of dye will be added to fixed amounts of protein in buffered solutions. The reaction mixture will be subjected to gel filtration to separate the dye-protein complex from free, unbound dye. Two types of binding studies can be completed ... 

In the virtually ignored study by Dai (with three nonself citations in five years) [521], the paper by Graham [451] is not cited either, but the key issue is both identified and clarified. Based on the results summarized in Fig. 21, the author concluded that electrostatic interaction between cationic dyes and the surface of activated carbon has a great effect on adsorption capacity. Below the isoelectric point of the activated carbon (when the positive zeta potential was above 60 mV), the capacity is significantly reduced due to electrostatic repulsion between cationic dyes and the carbon surface. In a follow-up study, while still failing to acknowledge earlier important contributions to the resolution of the key issues, Dai [522] reinforced and confirmed the electrostatic attraction vs. repulsion arguments. The author used anionic dyes (phenol red, carmine, and titan yellow) and... 

Another mutation involved replacement of Glu-212 by Gln-212. also carried out by Rongey et al.. The mutant shows an initial rapid oxidation of three cytochrome molecules, followed by a -30 times lower rate [Fig. 8 (E)]. This result suggests that the site for the second proton-uptake, H (2), is blocked. Separate proton-uptake measurements using the pH-sensitive dye phenol red showed the uptake of the... 

Kinetics of Proton Uptake. The Rinetics of proton uptaRe were measured for both native and mutant RCs using the pH indicator dye phenol red as described in Sec. 3. In RCs of Rb. sphaeroides R-26, 2.0 H /Qb" were taRen up within the experimental time resolution (Fig. 

To follow the way of the seemingly non-released protons, we measured the proton uptake at the reduction site of photosystem II via absorption changes of the pH indicating indicator dye phenol red at 559 nm. In control thylakoids (circles in Fig.2) we observed nearly the same proton uptake at every flash. 

B) Measurements with pH-in cating dye phenol red at 559 nm, indicating pH-changes in the suspending medium. Open squares CF -depleted tylakoids. Filled squares same material, but after incubation with DCCD. TTie... 

Figure 16 Examples of dyes used by Suslick et al. in array sensing of beverages, (a) A metalloporphyrin dye, (b) a solvatochromic dye (Reichert s), (c) and a pH indicator dye (phenol red).

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