Behaviour of cetyltrimethylammonium bromide, Triton X-100 and Triton X-114 in mixed monolayer at the (water–air) interface

2014 ◽  
Vol 69 ◽  
pp. 85-92 ◽  
Author(s):  
Katarzyna Szymczyk ◽  
Anna Zdziennicka ◽  
Joanna Krawczyk ◽  
Bronisław Jańczuk
2013 ◽  
Vol 59 ◽  
pp. 35-42 ◽  
Author(s):  
Katarzyna Szymczyk ◽  
Anna Zdziennicka ◽  
Joanna Krawczyk ◽  
Bronisław Jańczuk

Molecules ◽  
2021 ◽  
Vol 26 (14) ◽  
pp. 4313
Author(s):  
Bronisław Jańczuk ◽  
Katarzyna Szymczyk ◽  
Anna Zdziennicka

Measurements were made of the surface tension of the aqueous solutions of p-(1,1,3,3-tetramethylbutyl) phenoxypoly(ethylene glycols) having 10 oxyethylene groups in the molecule (Triton X-100, TX100) and cetyltrimethylammonium bromide (CTAB) with Zonyl FSN-100 (FC6EO14, FC1) as well as with Zonyl FSO-100 (FC5EO10, FC2) ternary mixtures. The obtained results were compared to those provided by the Fainerman and Miller equation and to the values of the solution surface tension calculated, based on the contribution of a particular surfactant in the mixture to the reduction of water surface tension. The changes of the aqueous solution ternary surfactants mixture surface tension at the constant concentration of TX100 and CTAB mixture at which the water surface tension was reduced to 60 and 50 mN/m as a function of fluorocarbon surfactant concentration, were considered with regard to the composition of the mixed monolayer at the water-air interface. Next, this composition was applied for the calculation of the concentration of the particular surfactants in the monolayer using the Frumkin equation. On the other hand, the Gibbs surface excess concentration was determined only for the fluorocarbon surfactants. The tendency of the particular surfactants to adsorb at the water-air interface was discussed, based on the Gibbs standard free energy of adsorption which was determined using different methods. This energy was also deduced, based on the surfactant tail surface tension and tail-water interface tension.


1981 ◽  
Vol 59 (7) ◽  
pp. 469-476 ◽  
Author(s):  
F. B. St. C. Palmer

The phosphatase which specifically removes one phosphate group from phosphatidyl-myo-inositol 4,5-bisphosphate was purified up to 6000-fold from the cytosol of the protozoan Crithidia fasciculata. Lipoproteins which interfere with the purification were precipitated by reducing the pH to 4.5. The enzyme was isolated from the supernatant by ammonium sulfate fractionation, gel filtration (Sepharose CL-6B), ion–exchange chromatography (DEAE-Sepharose CL-6B), and hydrophobic chromatography on detergent-saturated phenyl-Sepha-rose CL-4B. The preparations had specific activities of 44–110 μmol∙min−1∙mg protein−1 with phosphatidyl-myo-inositol 4,5-bisphosphate, but were inactive with a variety of lipid and nonlipid phosphate esters. The enzyme was stable in the presence of salt and exhibited a relative mass of 117 000. It formed larger aggregates in the absence of salt and was dissociated into monomers of relative mass 57 000 by sodium dodecyl sulfate.Addition of Triton X-100 to the assay mixture reduced the dependence upon moderation of the charge of the substrate by cetyltrimethylammonium bromide. In the presence of both detergents the Mg2+ dependence of the enzyme was reduced (Km for Mg2+ = 40 μM) while the "apparent" Km for the substrate was unchanged at 240 μM. Substrate precipitation at higher Mg2+ concentrations was eliminated.


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