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Compared with FTMS

Further control experiments were performed to find out if other proteins also bind to the DNA aptamers. All proteins used as controls—human serum albumin (p/ 4.9), bovine serum albumin (p7 4.7), myoglobin (p7 7.3), and mutarotase, 10 ftM each—showed negligible binding to the aptamer compared with cytochrome c (p7 10.65). At least by comparison with these few proteins, cytochrome c binding to DNA aptamers can be regarded as specific, although this specificity could simply reflect the p7 value of the protein. [Pg.93]

Table 1 shows typical emittance data for two devices. The emittance data may be compared with the variation observed in extant mechanical louvers, ca. 0.16 to 0.56 Ae = 0.4) (3). We also note that, to the best of our knowledge, these dynamic range (i.e. light/dark electrochromic contrast) values, e.g. > 50% Reflectance at 3 to 12 ftm (Figure 3) and Ae> 0.5 (Table I), represent the largest dynamic (i.e. switchable) IR signature variation in arsy material... [Pg.71]

Fig. 10.6. MALDI-FTMS determination of a common industrial polymer, polyoxypropylenediamine (top). The oligomers observed are cationized by sodium attachment and the average molecular mass information is shown in the middle spectrum. The manufacturer s specification of average molecular mass corresponding to 33.1 (mass 2170) repeating units agrees with the ma.ss distribution of 2193. TTie measured isotopic peak distribution for the n = 33 oligomer is compared with the theoretical isotopic distribution in the bottom spectrum. (Source Ref. [37, fig. 2].)... Fig. 10.6. MALDI-FTMS determination of a common industrial polymer, polyoxypropylenediamine (top). The oligomers observed are cationized by sodium attachment and the average molecular mass information is shown in the middle spectrum. The manufacturer s specification of average molecular mass corresponding to 33.1 (mass 2170) repeating units agrees with the ma.ss distribution of 2193. TTie measured isotopic peak distribution for the n = 33 oligomer is compared with the theoretical isotopic distribution in the bottom spectrum. (Source Ref. [37, fig. 2].)...
The clustering reactions of SiD + (n = 0-3) and Si2D + (n = 0-6) cations with deuterated disilane, Si2D6, have been measured in a FTMS study110. The dominant pathway for these reactions was found to correspond to silylene transfer and SiD4 elimination. The overall reactivity of disilane compared to monosilane was found to be higher, and this was explained by the fact that the silicon-silicon bond in disilane is considerably weaker (76 kcalmol-1) than the Si—H bond of SiFLt (88 kcalmol-1)111. Thus the insertion of Si+ into the Si—Si bond was calculated to be 17 kcalmol-1 more favorable than Si+ insertion into the Si—H bond of SiFFt106,112. [Pg.1119]

Although there are many attractive features of Fourier transform mass spectrometry (FTMS), there are problems with current implementations. The FT mass spectrometer is still a relatively young instrument when compared to the double-focussing mass spectrometer, and comparisons of the spectrometers and their... [Pg.34]

The sensitivity of FTMS is also comparable to that of sector instruments. Although sector instrument detectors can be used to count single ions and FTMS detectors cannot, both methods will yield a peak profile for approximately 100 ions. Detecting a single ion in organic or bioanalytical chemistry is of limited utility because its mass cannot be assigned with any certainty. [Pg.36]

The method of choice is dependent upon the analyte, the assay performance required to meet the intended application, the timeline, and cost-effectiveness. The assay requirements include sensitivity, selectivity, linearity, accuracy, precision, and method robustness. Assay sensitivity in general is in the order of IA > LC-MS/MS > HPLC, while selectivity is IA LC-MS/MS > HPLC. However, IA is an indirect method which measures the binding action instead of relying directly on the physico-chemical properties of the analyte. The IA response versus concentration curve follows a curvilinear relationship, and the results are inherently less precise than for the other two methods with linear concentration-response relationships. The method development time for IA is usually longer than that for LC/MS-MS, mainly because of the time required for the production and characterization of unique antibody reagents. Combinatorial tests to optimize multiple factors in several steps of some IA formats are more complicated, and also result in a longer method refinement time. The nature of IAs versus that of LC-MS/MS methods are compared in Table 6.1. However, once established, IA methods are sensitive, consistent, and very cost-effective for the analysis of large volumes of samples. The more expensive FTMS or TOF-MS methods can be used to complement IA on selectivity confirmation. [Pg.155]

Comparing FTMS with Fourier transform nuclear magnetic resonance (FTNMR), we first notice how the frequency range to be covered here is very large. Second, relaxation in NMR is invariably linked with the interaction among liquid-phase or solid-phase molecules. In the gas phase, relaxation depends on the vacuum and on the stability of the ions being observed. If the vacuum is not sufficient, collisions slow the ions and their movement becomes incoherent. The observation of an ion is also limited to its lifetime. [Pg.161]

Reversibility of Reduction of Intracellular Extrachromosomal HBV DNA Additional experiments were then performed to assess the reversibility of ddC-inhibited expression of intracellular extrachromosomal HBV DNA. As shown by the Southern blot analyses presented in Figure 2, synthesis of intracellular extrachromosomal HBV DNA was completely inhibited after a six day treatment with ddC at all concentrations tested, including the lowest concentration, 100 ftM (Lanes 14-22). The expression of intracellular extrachromosomal HBV DNA, compared to DMSO-treated cells (Lanes 11-13, arrows), recovered after removal of ddC (Lanes 25-33, arrows). DNA obtained from HepG2 cells (Lane 8) presented no band corresponding to HBV DNA. [Pg.545]


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