Accurate fluorescent polymeric thermometers containing an ionic component

The Analyst ◽  
2007 ◽  
Vol 132 (2) ◽  
pp. 121-126 ◽  
Author(s):  
Chie Gota ◽  
Seiichi Uchiyama ◽  
Tomohiko Ohwada
Keyword(s):  
1979 ◽  
Vol 6 (3) ◽  
pp. 323 ◽  
Author(s):  
M.J Beilby ◽  
H.G.L Coster

Voltage-clamp experiments over a wide range of clamp potentials were made with cells of C. corallina using a fast voltage-clamp apparatus. Clamps of the plasmalemma potential in the range - 170 mV to - 70 mV revealed a large transient inward current which followed the usual chloride current transient hitherto described in the literature. This additional component decreased in amplitude and occurred earlier in the clamp as the clamp potentials were made more positive up to ~ -70 mV. For clamp potentials > - 50 mV, a large, prompt, outward current appeared. The additional current transients could not be observed in vacuolar potential clamp experiments, except at clamps � - 10 mV. The effects of changes in the external Cl- and Ca�+ concentrations with plasmalemma clamps at various potentials suggest that the additional transient here reported consists of a flow of Ca�+ ions and also reaffirms the identification of the other transient with a flow of Cl- ions. Reversal of the additional current transient when the clamp potential is sufficiently large (i.e. at large depolarization), places the equilibrium potential of the ionic component responsible for this transient at - 50 mV (� 20 mV). Estimates, based on this equilibrium potential, of the cytoplasmic Ca�+ concentration yield unrealistic values. Possible answers to this dilemma are discussed.


1971 ◽  
Vol 38 (1) ◽  
pp. 9-23 ◽  
Author(s):  
Margaret L. Green

SummaryThe specificity of the interaction betweenκ-casein,αs-casein andβ-casein which forms the basis of micelle stabilization was studied by investigating the extent to whichκ-casein could be replaced by other proteins. Of those tested, only gelatin replacedκ-casein and even it was only 2·5% (w/v) as effective and required a long pre-incubation period. The micelles formed by each ofκ-casein and gelatin withαs-casein and Ca2+were of a similar size to the casein—Ca complexes which compose natural micelles. Gelatin also formed complexes withαs- and withβ-casein at 30°C in the absence of CaCl2. Evidence was obtained that the interactions between gelatin and the caseins had a much stronger ionic component than had those betweenκ-casein and the other caseins. It was concluded that the interactions betweenκ-casein andαs- andβ-caseins which lead to micelle formation are highly specific and probably involve definite sites in each molecule.


2020 ◽  
Vol 11 (3-2020) ◽  
pp. 62-68
Author(s):  
A. S. Genevskaya ◽  
◽  
G. V. Mitrofanova ◽  
◽  

Adsorption at the gas —air interface and micelle formation in binary solutions of ethoxylated alkyl phenol (Neonol AF 9-10) and sodium oleate have been studied. The Rubin and Rosen equations were used to determine the interaction parameters and the composition of mixed micelles and adsorption layers depending on the initial solution composition. The authors have found out that the micelles and the adsorption layer at the interface are enriched in a non-ionic component. The maximum synergistic effect during micelle formation was found for solutions containing 20–30 % molar of reagent Neonol AF 9-10, and during adsorption —20 and 50 %.


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