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Conventional mixing method

The uniform dispersion of short carbon fibres, particularly at higher fibre volumes, is difficult. The most that can be added using conventional mixing methods and materials is about 1% by volume. The dispersion of the fibres into individual filaments is controlled by the mixing technique. The methods used have included ... [Pg.400]

The equilibrium binding constant for this 1 1 association is Xu = ki/lLi. The Xu values were measured spectrophotometrically, and the rate constants were determined by the T-jump method (independently of the X,j values), except for substrate No. 6, which could be studied by a conventional mixing technique. Perhaps the most striking feature of these data is the great variability of the rate constants with structure compared with the relative insensitivity of the equilibrium constants. This can be accounted for if the substrate must undergo desolvation before it enters the ligand cavity and then is largely resolvated in the final inclusion complex. ... [Pg.152]

At the beginning of this chapter we pointed out that the rate of mixing of two solutions places a limit on the fastest reactions that can be studied by conventional kinetic methods. In this section we explore the fastest mixing methods that have been devised. These methods therefore constitute a specialized, but otherwise continuous, extension of conventional kinetics into the fast reaction range. [Pg.176]

The void fraction data obtained in micro-channels and conventional size channels showed significant differences depending on the channel cross-section and inlet geometry. For the micro-channel with a diameter of 100 pm, the effects of the inlet geometry and gas-liquid mixing method on the void fraction were seen to be quite strong, while the conventional size channels have shown a much smaller effect of inlet geometry on the void fraction. [Pg.250]

This section deals briefly with classical methods based on conventional mixing of the sample and reagents such as the batch mode and low-pressure flow mixing methods, as well as the use of CL detection in continuous separation techniques such as liquid chromatography and capillary electrophoresis for comparison with the unconventional mixing mode. [Pg.180]

The CVD catalyst exhibits good catalytic performance for the selective oxidation/ammoxida-tion of propene as shown in Table 8.5. Propene is converted selectively to acrolein (major) and acrylonitrile (minor) in the presence of NH3, whereas cracking to CxHy and complete oxidation to C02 proceeds under the propene+02 reaction conditions without NH3. The difference is obvious. HZ has no catalytic activity for the selective oxidation. A conventional impregnation Re/HZ catalyst and a physically mixed Re/HZ catalyst are not selective for the reaction (Table 8.5). Note that NH3 opened a reaction path to convert propene to acrolein. Catalysts prepared by impregnation and physical mixing methods also catalyzed the reaction but the selectivity was much lower than that for the CVD catalyst. Other zeolites are much less effective as supports for ReOx species in the selective oxidation because active Re clusters cannot be produced effectively in the pores of those zeolites, probably owing to its inappropriate pore structure and acidity. [Pg.246]

Fig. 5. Compatibility of Binding Proteins on Commercial Available Solid Materials. Each affinity resins bearing benzensulfonamide (10 ml) was mixed with 1 ml of rat brain lysate (total protein 8 mg/mL, in 0.25 M sucrose, 0.3 mM DDC, 25 mM Tris-HCI 7.6), respectively. Specific binding protein, CA2 in this case, was identified by the SAC method described in Subheading 3.2 instead of conventional competition method because of low solubilify of fhe compound. After washed with 1 ml of lysate buffer (0.25 M sucrose, 0.3 mM DDC, 25 mM Tris-FICI pFI 7.6), fhe binding proteins were eluted SDS sample buffer (Nacalai s SDS sample buffer (x3), 30566-22), and then analyzed. Fig. 5. Compatibility of Binding Proteins on Commercial Available Solid Materials. Each affinity resins bearing benzensulfonamide (10 ml) was mixed with 1 ml of rat brain lysate (total protein 8 mg/mL, in 0.25 M sucrose, 0.3 mM DDC, 25 mM Tris-HCI 7.6), respectively. Specific binding protein, CA2 in this case, was identified by the SAC method described in Subheading 3.2 instead of conventional competition method because of low solubilify of fhe compound. After washed with 1 ml of lysate buffer (0.25 M sucrose, 0.3 mM DDC, 25 mM Tris-FICI pFI 7.6), fhe binding proteins were eluted SDS sample buffer (Nacalai s SDS sample buffer (x3), 30566-22), and then analyzed.

See other pages where Conventional mixing method is mentioned: [Pg.144]    [Pg.181]    [Pg.321]    [Pg.346]    [Pg.2331]    [Pg.144]    [Pg.181]    [Pg.321]    [Pg.346]    [Pg.2331]    [Pg.394]    [Pg.26]    [Pg.33]    [Pg.342]    [Pg.214]    [Pg.464]    [Pg.237]    [Pg.177]    [Pg.332]    [Pg.103]    [Pg.372]    [Pg.444]    [Pg.275]    [Pg.195]    [Pg.223]    [Pg.403]    [Pg.80]    [Pg.452]    [Pg.182]    [Pg.214]    [Pg.116]    [Pg.14]    [Pg.237]    [Pg.220]    [Pg.91]    [Pg.9]    [Pg.226]    [Pg.214]    [Pg.157]    [Pg.160]    [Pg.575]    [Pg.26]    [Pg.33]    [Pg.609]    [Pg.992]    [Pg.142]    [Pg.182]   
See also in sourсe #XX -- [ Pg.346 ]




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