Mutual influence of cetyltrimethylammonium bromide and Triton X-100 on their adsorption at the water–air interface

2013 ◽  
Vol 59 ◽  
pp. 35-42 ◽  
Author(s):  
Katarzyna Szymczyk ◽  
Anna Zdziennicka ◽  
Joanna Krawczyk ◽  
Bronisław Jańczuk
Keyword(s):  
Cetyltrimethylammonium Bromide ◽  
Mutual Influence ◽  
Air Interface ◽  
Triton X

scholarly journals Adsorption Properties of Hydrocarbon and Fluorocarbon Surfactants Ternary Mixture at the Water-Air Interface

Molecules ◽  
2021 ◽  
Vol 26 (14) ◽  
pp. 4313
Author(s):  
Bronisław Jańczuk ◽  
Katarzyna Szymczyk ◽  
Anna Zdziennicka
Keyword(s):  
Surface Tension ◽  
Water Surface ◽  
Standard Free Energy ◽  
Ternary Mixtures ◽  
Free Energy Of Adsorption ◽  
Interface Tension ◽  
Air Interface ◽  
Surface Excess Concentration ◽  
Tail Water ◽  
Triton X

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.

The phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase from Crithidia fasciculata

1981 ◽  
Vol 59 (7) ◽  
pp. 469-476 ◽  
Author(s):  
F. B. St. C. Palmer
Keyword(s):  
Cetyltrimethylammonium Bromide ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Phosphate Esters ◽  
Relative Mass ◽  
Crithidia Fasciculata ◽  
Specific Activities ◽  
Triton X

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.

scholarly journals Evidence that eosinophils catalyze the bromide-dependent decarboxylation of amino acids

Blood ◽  
1981 ◽  
Vol 58 (6) ◽  
pp. 1112-1118
Author(s):  
R Cramer ◽  
MR Soranzo ◽  
P Patriarca
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Guinea Pig ◽  
Aspartic Acid ◽  
Cetyltrimethylammonium Bromide ◽  
Human Neutrophils ◽  
Cationic Detergent ◽  
Nonionic Detergent ◽  
Normal Human ◽  
Triton X

Human eosinophils from subjects with or without myeloperoxidase (MPO) deficiency and guinea pig eosinophils are able to decarboxylate L- alanine in the presence of the cationic detergent cetyltrimethylammonium bromide (CTAB) but not in the presence of the nonionic detergent Triton X-100. Instead, both normal human neutrophils and guinea pig neutrophils decarboxylate L-alanine in the presence of either detergent. When the non-bromide-containing cationic detergent cetyltrimethylammonium hydroxide (CTAOH) is used instead of CTAB, the eosinophils from MPO-deficient subjects are unable to decarboxylate L- alanine. Decarboxylation occurs with the combination CTAOH-Br-, but not with the combinations CTAOH-I-, CTAOH-CI-, or CTAOH-F-. Bromide in the absence of CTAOH does not promote decarboxylation. Triton X-100 and deoxycholate are much less effective in promoting decarboxylation in the presence of bromide. L-Lysine and L-aspartic acid are decarboxylated to a considerably lower rate than L-alanine in the presence of CTAOH and Br-. It is concluded that the eosinophils can catalyze the bromide-dependent decarboxylation of the apolar amino acid L-alanine in the presence of a cationic detergent.

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