Tritonal preparation

The 77 K absorption spectrum (a) and the 4th derivative (b) of the purified PSII reaction center complex prepared by isoelectric focusing in digitonin solution are shown in Fig. 2. The spectrum is well-resolved than in Triton preparation (1). Absorption in the red maximum region, as well as the peaks around 600 nm, is clearly separated into two components 670 and 680 nm in the red, which might be attributed to the accessory chlorophyll and P-680 plus pheophytin acceptor, respectively. The 77 K emission spectrum of Triton preparation (1) exhibits shoulders on both sides of the main peak at about 681 nm, originating from free chlorophyll and the aggregates. However, the contribution of these components was markedly reduced in the spectrum of the complex prepared by the present procedure a sharp emission peak at about 683 nm was observed in this case. 

In contrast to the Triton preparation (1) which loses the activity of pheophytin photoreduction under steady-state illumination within 5 hr at room temperature (25 C ) > the complex obtained here is relatively stable and keeps the activity more than 100 hours at 30 °C as shown in Fig. 4. The stabilization can also be attained just by exchanging Triton X-100 to dodecylmaltoside. However, the complex is still unstable when exposured to light this may be correlated to the high probability of P-680 formation in this kind of preparations. 

Two methods of sample preparation were investigated. The former is dilution of blood semm with 0.1% Triton X-100, the latter is aeid mierowave digestion. As evaluated, the most adequate mineralization proeedure for determining the majority of elements in blood semm by ICP AES is aeid mierowave digestion. However, the ICP AES determination of abundant elements (B, Si, Mn), whieh present in semm at 0.001-0.01 ppm levels should be follow sample dilution with Triton X-100. 

Benzyltrimethylammonium hydroxide (Triton B) [100-85-6] M 167.3, d 0.91. A 38% soln (as supplied) was decolorized (charcoal), then evaporated under reduced pressure to a syrup, with final drying at 75° and 1 mm pressure. Prepared anhydrous by prolonged drying over P2O5 in a vacuum desiccator. 

As a precautionary measure to prevent the appearance of maxima, sufficient gelatin to give a final concentration of 0.005 per cent should be added. The gelatin should preferably be prepared fresh each day bacterial action usually appears after a few days. Other maximum suppressors (e.g. Triton X-100 and methyl cellulose) are sometimes used. 

Triton X-100, like gelatin, suppresses both positive and negative maxima, but, unlike gelatin, its aqueous solution is stable. A stock 0.2 per cent solution is prepared by shaking 0.20 g of Triton X-100 thoroughly with 100 mL of water. About 0.1 mL of this solution should be added to each 10 mL of the sample solution to give a Triton X-100 concentration of 0.002 per cent. 

The luciferin-luciferase reaction of Arachnocampa was first demonstrated by Wood (1993), by mixing a cold-water extract and a cooled hot-water extract. The cold-water extract was prepared with 27 mM Tricine, pH 7.4, containing 7mM MgSC>4, 0.2 mM EDTA, 10% glycerol and 1% Triton X-100, and incubated with 1 mM ATP on ice for 18 hr. The hot-water extract was prepared by heating the cold water extract before the addition of ATP at 98°C for 5 min. The luminescence reaction was performed in the presence of 1 mM ATP. 

Epoxyeyclohexanone has been prepared in 30% yield4 by epoxi-dation of 2-cyclohexen-l-one with alkaline hydrogen peroxide, using a procedure described for isophorone oxide (4,4,6-trimethyl-7-oxabicyclo[4.1.0]heptan-2-one).5 A better yield (66%) was obtained using f r/-butyl hydroperoxide (1,1-dimethylethylhydroperoxide) and Triton B in benzene solution.6 The procedure described here is simple and rapid. 

Sometimes it can be advantageous to use mixtures of alkanesulfonates and nonionic surfactants, such as Triton X-100, to prepare monodisperse polystyrene particles [95]. 

Figure 4. Purification of PemB from E. coli K38 pGPl-2/pPME6-5 cells. Proteins were separated by urea-SDS-PAGE. Lane 1, induced cell lysate lane 2, soluble protein fraction from induced cells lane 3, membrane fraction from non-induced cells lane 4, membrane fraction from induced cells lane 5, membrane proteins not extracted by Triton X-100 lane 6, membrane proteins extracted by Triton X-100 lane 7, PemB purified by preparative electrophoresis. The molecular weight standard positions are indicated.

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]. 

Prepare a 1 40 dilution of stock Giemsa stain in neutral buffered water, pH 7.0 to 7.2 (generally, 2 ml of Giemsa stock plus 38 ml of buffered water with 0.01% Triton X-100). 

After 2 h incubation of the prepared antibody beads with UV-crosslinked extract in a cold room, the beads are washed 4 x with 100 /A RIPA buffer (50 mMTris-HCl pH 7.5, 150 rnMNaCl, 1% NP-40, 0.5% sodium deoxycholate, and 0.1% SDS) and lx with genomic DNA lysis buffer (50 mM Tris, pH 7.4, 10 mM EDTA, 500 mM NaCl, 2.5 mM DTT, 0.5 mM spermidine, 1% Triton X-100). Approximately 300 /(I of PK solution (1 mg/ml proteinase K in genomic DNA lysis buffer and 0.2 U//A RNase inhibitor) is added to the total lysate previously kept on ice and the beads are then incubated at 37° for 30 min. Gently flick the tubes to resuspend the beads every 10 min during the incubation. After removal of the proteinase K solution, 300 /A of RNA extraction solution (4 M guanidine thiocyanate, 0.5% sarkosyl, and 25 mM sodium citrate, pH7) is added to the beads, incubated for 10 min and the supernatant is mixed with 30 fig yeast tRNA (as a carrier) and 30 fil of 3 M sodium acetate. The RNA solution is phenol-chloroform extracted, ethanol-precipitated, and the pellet washed once with 70% ethanol. The dry pellet is used for 1st strand cDNA synthesis, followed by PCR analysis. The removal of proteins... 

Prepare a solution consisting of 2.5 ml glycerol, 100 pi of 10 percent Triton X-100 (Thermo Fisher Surfact-Amps X-100), and 10 pi 2-mercaptoethanol. 

Prepare a chitin affinity column by washing with at least 10 bed volumes of 25 mM HEPES, 250mM NaCl, ImM EDTA, 0.1 percent Triton X-100, pH 7.0 (wash buffer). 

Di-(2-acetoxyethyl) A-(4-fluorophenyl)aminomethylenemalonates (47) were prepared in the reaction of 3-substituted 4-fluoroaniline and di-(2-acetoxyethyl) ethoxymethylenemalonate in the presence of Triton B under... 

A Working Solution of the stain should be prepared just before use, by combining 10 ml of 0.1% Triton X-100 in phosphate-buffered saline, 2 mg RNase (DNase-free, Sigma), and 200 pi PI solution (Sigma, 1 mg/ml in distilled water). Stock solutions of Triton X-100 and PI should be stored at 4°C. Centrifuge the ethanol-fixed cells (200 x g for 5 min) and discard the supernatant, removing it completely. 

In order to more closely represent the volatilization environment that would be encountered in an evaporation pond, Triton X-100, a non-ionic emulsifier similar to those used in some pesticide formulations, was added to prepared pesticide solutions at 1000 ppm. The presence of this emulsifier caused a decrease in the percent pesticide volatilized in one day in all cases except for mevinphos (Table VI). Three mechanisms are probably in operation here. First, Triton X-100 micelles will exist in solution because its concentration of 1000 ppm is well above its critical micelle concentration of 194 ppm (30). Pesticide may partition into these micelles, reducing the free concentration in water available for volatilization, which will in turn reduce the Henry s law constant for the chemical (31). Second, the pesticides may exhibit an affinity for the thin film of Triton that exists on the water surface. One can no longer assume that equilibrium exists across the air-water interface, and a Triton X-100 surface film resistance... 

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