TRITON sequence

Of particular interest for nonproprietary use is the SCALE system, developed at ORNL, which has the SAS2 and TRITON sequences that are available to perform Steps 2-5 (with Step 1 results already embedded in the cross sections libraries provided). Adding to this capability with a diffusion theory code (e.g., VENTURE) and a kinetics code (e.g., SKINATH) gives the general analyst capability of performing basic reactor analysis. 

Figure 10 Mismatch detection by using a chemiluminescent AE-labeled cDNA probe. Procedure [9, 11] Acridinium ester-labeled probes specific for either wild-type or mutant sequence corresponding to a target DNA are hybridized with the sample DNA for 1.0 h at 60°C in a hybridization buffer (pH 5.2). Hybridized and nonhybridized probes are discriminated by the hydrolysis reaction for 12 min at 62.5°C in the presence of Na2B407 (pH 8.5) and Triton X-100. The chemiluminescence of each sample is then measured in a luminometer.

The N-terminal amino acid sequence of both of these polypeptides has been determined [11,12]. Polypeptides of 7, 6.5, 5.5 and 5 kDa have been shown to be associated with a spinach PS II preparation [13]. The three larger polypeptides are hydrophobic, as shown by partitioning in Triton X-114, and are presumed to be intrinsic membrane proteins. The 5 kDa polypeptide is hydrophilic and therefore presumably peripheral to the core complex. This polypeptide has been purified and its amino acid composition determined [13]. 

BSA, dithiothreitol and hydrogenated Triton X-100 were purchased from Calhiochem. Urea was from Pierce. lodoacetamide was from Sigma and 4-vinylpyridine was from Aldrich. Ammonium hicarhonate was from Fisher. Sequencing grade endoproteases Lys-C and trypsin were from Boehringer Mannheim. 

Two conditions were realized in the wind wave facility in the first set of experiments the interface was clean, whereas in the second set a surfactant (Triton-X-100, concentration 3 ppm) was used. Image sequences of duration of 1 second (60 frames at 60 Hz) were recorded every 10 seconds for a time period of 50 minutes. This procedure was repeated at four different wind speeds. Using the controllable air ventilation system in the wind wave facility, the latent heat flux was switched on and off every 5 minutes. The net loss of heat at the water surface was determined by the rate of change of the overall water bulk temperature (Schimpf 2000). 

Another cytochrome c, cytochrome c-550(m), was purified from the bacterium with the aid of the detergent, Triton X-100 (Nomoto et al., 1993). This cytochrome spectrally resembles cytochrome c-550(s), while the N-terminal amino acid sequence differs between them. Its molecular mass is 13.6 kDa. 

In order to avoid a pronounced shift of the phase behaviour with the progress of the reaction one reactant can be fed to the reactor in a semi-batch mode. With this concept shift in phase behaviour may be compensated and the optimal state of the system is maintained during the whole reaction time. After phase separation at the most suitable temperature conventional product isolation follows. This sequence of process steps is also possible in a continuously operating process, as illustrated in Fig. 5.17 for the synthesis of 1-phenoxyoctane in a microemulsion stabilised by Triton X-100 [28],... 

Fig. 6. Time sequence (45 s/image) taken on n-Si(l 11) tilted by 0.7° in Triton/NaOH. Chemical etching is promoted between images 2-6. In other images the surface is cathodically protected. Frames are 1400x1400 (after [18]).

Optimal activity of the purified enzyme solubilized in Triton X-100 is obtained in the presence of excess phospholipids. The pH optimum of the steady-state reaction with horse heart ferrocytochrome c occurs at pH 6, yielding a turnover of about 80 electrons/sec, similar to the value obtained for the enzyme from P. denitrificans. Remarkably, a purified membrane-bound c cytochrome, identified by its N-terminal sequence as cytochrome Ci from the 6c 1 complex, stimulates the rate of electron transfer between horse heart c5d ochrome c and the cytochrome c oxidase by about a factor of two. The in vitro enzyme assay with purified cytochrome oxidase and reduced amicyanin showed no activity only after the addition of endogenous cytochrome C550 (or horse heart cjfto-chrome c) did oxidation of amicyanin occur, in agreement with the sequence of electron transfer ami — cjft C550 CCO. 

On the basis of the results just described, Bayer and coworkers [229] proposed a solvent system, referred to as magic mixture [2 N ethylene carbonate in DMF-DCM-NMP (1 1 1) containing 1% Triton X-100 at 50°C], that was effective for the synthesis of peptides containing difficult sequences. This system incorporates DMF, NMP, and ethylene carbonate to break the a-helical and j8-sheet structures and DCM and the nonionic detergent to mediate in the aggregation of the hydrophobic peptide chains. 

The fluidity in the neighborhood of probe molecules can be tested by use of probes capable of intramolecular excimer formation. The probe molecules contain the two excimer-forming moieties linked by an alkyl chain. The extent of excimer formation depends on the viscosity of the environment and can be monitored by measuring the excimer/monomer fluorescence intensity ratio. The dependence of this ratio on reciprocal viscosity for the probe molecule dipyrenylpropane is shown in Fig. 18, in which the obtained microfluidities for surfactant systems are indicated. The fluidities decrease in the order SHS microemulsion, SDS, CTAC, Triton X-100 cf. Ref. 167 (for abbreviations see Tables 6 and 7). The same sequence order was found by Kano et al. (68). In systems containing heavy counterions the method leads to data that must be evaluated carefully, since heavy atom interactions may be different with excited monomers and excimers. The intramolecular excimer technique is also useful in biological studies. For instance, Almeida et al. investigated the sarcoplasmic reticulum membrane in which the activity of the Ca -pumping enzyme is modulated by the membrane fluidity (197). 

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