Tritonal analytical

In the present work it was studied the dependence of analytical characteristics of the composite SG - polyelectrolyte films obtained by sol-gel technique on the content of non-ionic surfactant in initial sol. Triton X-100 and Tween 20 were examined as surfactants polystyrene sulfonate (PSS), polyvinyl-sulfonic acid (PVSA) or polydimethyl-ammonium chloride (PDMDA) were used as polyelectrolytes. The final films were applied as modificators of glass slides and pyrolytic graphite (PG) electrode surfaces. 

PtRu nanoparticles can be prepared by w/o reverse micro-emulsions of water/Triton X-lOO/propanol-2/cyclo-hexane [105]. The bimetallic nanoparticles were characterized by XPS and other techniques. The XPS analysis revealed the presence of Pt and Ru metal as well as some oxide of ruthenium. Hills et al. [169] studied preparation of Pt/Ru bimetallic nanoparticles via a seeded reductive condensation of one metal precursor onto pre-supported nanoparticles of a second metal. XPS and other analytical data indicated that the preparation method provided fully alloyed bimetallic nanoparticles instead of core/shell structure. AgAu and AuCu bimetallic nanoparticles of various compositions with diameters ca. 3 nm, prepared in chloroform, exhibited characteristic XPS spectra of alloy structures [84]. 

Aguilera de Benzo Z, Fraile R, Carrion N, et al. 1989. Determination of lead in whole blood by electrothermal atomization atomic absorption spectrometry using tube and platform atomizers and dilution with Triton X-100. Journal of Analytical and Atmospheric Spectrometry 4 397-400. 

Figure 6.11 Polarogratn of a solution containing three analytes, showing three different waves . The half-wave potential, 1/2, for each is characteristic of the respective analyte couples, while the wave heights reflect the relative concentrations of each ion. The trace has been smoothed to remove the sawtoothed effects seen in Figures 6.7 and 6.8. The solution also contained KCl (0.1 mol dm ) as a swamping ionic electrolyte, and Triton X-lOO (a non-ionic surfactant) as a current maximum suppressor.

The magnitudes of these maxima can be decreased almost completely by adding a surfactant to the analyte solution - we call such an additive a current maximum suppresser (or, sometimes, a depolarizer). The usual suppresser employed is Triton X-1(X) (a non-ionic surfactant (detergent)), which is added to the solutions at concentrations of no more than 0.(X)2 mol dm. ... 

Analytical The composition of a sample of Tritonal is determined by extracting a weighed sample with benzene, drying and weighing the residue. The loss in wt represents TNT and the wt of residue represents Al (Ref 8)... 

In Table 8.1, cow s milk, breast milk, and infant formulae are considered together under the entry Milk and infant formulae, irrespective of the actual liquid or powdered form of the samples analyzed in each single study, because all these items share a similar matrix and pose analogous analytical problems. Triton X-100 has been used to measure Pb isotope ratios in milk powder samples prepared as slurries [39]. Simple dilution of fresh milk in alkaline media (in order to prevent protein precipitation) has also been successfully applied by other authors [40], especially for I determination [41-43], even though in most studies milk and infant formulae are analyzed following full digestion. 

Likewise, the luminescence properties of many analytes can be altered in the presenoe of surfactant aggregates (4,7.,8.). Consequently, addition of micelle-forming surfactants (present either in the LC mobile phase or added post-column) can improve the sensitivity of fluorimetric LC detectors (49,482). Micellar spray reagents have been utilized to enhance the fluorescence densitometric detection of dansylamino acids or polycyclic aromatic hydrocarbons (483). The effect was observed for TLC performed on cellulose or polyamide stationary phases with the micellar spray reagent being either CTAC, SB-12, or NaC (483). More recently, use of nonionic Triton X-100 has been found to improve the HPLC detection of morphine by fluorescence determination after post-column derivatization (486) as well as improve the N-chlorination procedure for the detection of amines, amides, and related compounds on thin-layer chromatograms (488). 

The most significant problem with the utilization of surfactant media in different separation schemes (particularly those at the preparative or process scales) concerns the recovery of the analyte from the surfactant media and subsequent recovery of the surfactant for re-use. Attempts to use extraction schemes with conventional organic solvents typically results in troublesome emulsion formation during the recovery steps. There are, however, several means available by which analytes can be recovered free of surfactant. These include the following (1) Several quick, gentle methods for the recovery of some analytes (usually proteins) from surfactant media (i.e. micellar NaLS, Triton X-100, CHAPS, deoxycholate, Brij-35) via use of column chromatography have been developed (509-515). Most of the stationary phase materials for this approach are available commercially (510,513). 

Baugh and King (43, 43a) have recently reported the isolation of a preparation from mitochondria with high NADH-ferricyanide and NADH-Q reductase activities (Table III). As compared to complex I, the preparation contains 20-25% less FMN, but more iron and labile sulfide, the ratio of FMN nonheme iron labile sulfide being 1 28 28. The enzyme is isolated from Keilin-Hartree particles (prepared from beef heart mitochondria) after treatment with Triton X-lOO and subsequently with cholate. It is claimed to be water soluble and free of phospholipids. However, satisfactory analytical data for the absence of lipid (e.g., phos-... 

IEF can also be carried out under denaturing conditions, for example in the presence of 9 M urea. For the analysis of hydrophobic proteins, non-ionic detergents such as Nonidet NP-40 or Triton X-100 can be added to the sample and the IEF gel. Analytical IEF is used to determine the pi of proteins, and also as a critical check of the homogeneity of protein preparations. The reprodudbility and resolving power of the technique is exploited in various applications where it is used to establish the identity and complexity of protein mixtures for example in food analysis, the origin of proteins in milk preparations, and in clinical analysis, determining the isoenzyme profile of apolipoproteins. 

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