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12 - substrates measuring

Sc 5) Measure affinity for substrate/Measure protein content 6) Perform feeding trials in animals. [Pg.352]

FIG. 1 FT-IR spectra in midfrequency region. DNA-treated gold substrate measured in reflection-absorption mode (a) and transmittance spectrum of DNA cast on Cap2 (b). [Pg.520]

Saito, S., Shinozaki, R., Suzuki, A. el al. (2003) SAE Papers, SP-1801 (Emissions Advanced Catalyst and Substrates, Measurement and Testing, and Diesel Gaseous Emissions) p. 209. [Pg.21]

A sensor array where different haptens are immobilized at well-defined areas on a plain glass surface has been developed [66], Using an automated flow injection system it was possible to incubate all areas on the chip with analytes, specific antibodies, secondary HRP-labeled antibodies, and CL substrate. Measurement of the light output via imaging performed with a CCD device allowed determination of the analytes present in the sample on the basis of the spatial localization of the CL signal. [Pg.493]

Odour will return in treated slurry as a result of post treatment fermentation. The concentration of readily fermentable substrates, measured as BOD5, provide an indicator of this problem. In continuous culture without oxygen limitation the BOD5 can be described by a model derived from the Monod (13) model of microbial growth (14). The supernatant BOD5 (g/1) from treatment at 15 to 45°C, was described by equation 3 and the whole BOD5 by equations 4 and 5(15). [Pg.301]

A 3/8 inch diameter aluminum or titanium-tungsten dot pattern WLs fabricated on top of the cured polyimide film to make electrical leakage to substrate measurements for pinhole density estimation. An etch decoration technique was used to visually determine pinhole densities in polyimide films. The polyimide film was cast on substrates comprised of a layer of 200 nm thick alumimmi on blue colored field oxide with a grid pattern for area computation. Replicate holes were etched in the aluminum by a hot phosphoric acid solution. With the polyimide film removed, a good visual contrast was achieved for pinhole density counting. [Pg.141]

Comparing catalytic effects of different modified polyethylenimines on the decarboxylation of nitrobenzisoxazole carboxylate, we can discern several interesting features. Comparison of the 25% laurylated polymer in the quaternized and nonquaternized forms, A and D, respectively, in Table X, shows that the former is about three times more effective as a catalyst than the latter. For the quaternized polymer the first-order catalytic constant k2 and the second-order rate constant nk2IKM are greater and the binding of substrate (measured by XM ) is stronger. [Pg.149]

A depth profile analysis of trace and matrix elements (B, Na, Ni, Fe, Mg, V, A1 and C) in a 26p.m Si layer on a SiC substrate measured by GDMS, yielded impurity profiles, for example, with constant Ni contamination in the Si layer and enrichment at the interface layer.45 However, with respect to depth profiling of thin layers using dc GDMS with a depth resolution between 50 and 500 nm, this technique plays a subordinate role compared to the commercially available and cheaper GD-OES (glow discharge optical emission spectrometry). [Pg.281]

Measured as in Basic Protocol 1 with casein substrate. Measured by the BCA protein assay of Smith et al. (1985). [Pg.367]

The solution was first filtered to remove particulate impurities and the films were heated to 80-85°C to remove the solvent. The thicknesses and refractive indices of the polymers were obtained from ellipsometric measurements on calibration layers, which were spun on BK7 glass substrates. Measurements on each sample were performed at four different wavelengths (63A.8 nm, 753.0 nm, 802.0 nm and 852 nm) in order to minimize the errors in the extrapolated... [Pg.266]

Highest sensitivity is reached when high enzyme activity within a thin layer is used and effective external mass transfer is provided. Under these conditions, substrate measurement can be managed down to the range of 1 micromolar with imprecision below 2 %. Therefore, owing to their limited sensitivity, "normal" enzyme electrodes are applicable only to metabolites present in the micro and millimolar concentration range. [Pg.23]

Figure 3. Relationship between the activation energy for diffusion in polystyrene and the molar volume of 10 organic substrates measured at temperatures greater than T. (Reproduced with permission from Ref. 4. Copyright 1976 Elsevier )... Figure 3. Relationship between the activation energy for diffusion in polystyrene and the molar volume of 10 organic substrates measured at temperatures greater than T. (Reproduced with permission from Ref. 4. Copyright 1976 Elsevier )...
Fig. 7.4. XRD 20 — io scans of PLD grown, nominally undoped ZnO thin films on c-plane (top), a-plane (center), and r-plane (bottom,) sapphire substrates, measured with Ni-filtered Cu-Ko, radiation. The ZnO films were grown at 0.01 mbar O2 and about 650° C... Fig. 7.4. XRD 20 — io scans of PLD grown, nominally undoped ZnO thin films on c-plane (top), a-plane (center), and r-plane (bottom,) sapphire substrates, measured with Ni-filtered Cu-Ko, radiation. The ZnO films were grown at 0.01 mbar O2 and about 650° C...
The correlation of two alternative measures of selectivity has recently been proposed as a mechanistic tool in solvolysis reactions (Pross and Koren, 1975). Thus a plot of the selectivities for a series of substrates measured both by competition between azide ion and water ( N /kw ), and by ethanol and water ( E/AW ) was found to be linear and of unit slope. This result strongly reinforces the view that... [Pg.101]

Table 1. The effect of 1 mM NaF + 20 pM A1C13 on the acetylcholinesterase activity (AChE) in freshly prepared intact RBC and in hemolysate of patients with AD (mean age 72.5 5.1 years), age-matched healthy controls (AM-HS) (72.1 1.6 years), and the group of young healthy subjects (YS) (35.9 8.5 years). Whole venous blood samples were drawn from each subject after overnight fasting., always at 07 30 AM. Red blood cells (RBC) were isolated from the blood of patients with AD, AM-HS, and YS by centrifugation [68], RBC AChE activity was evaluated in intact freshly prepared RBC or hemolyzate following the spectrophotometric method [45] with modifications. Buffer was Tris-HCl, pH 7.5 in the solution of 154 mmol L 1 NaCl, acetylthiocholine iodide was a substrate. Measurement of enzymatic activity was performed in fluorimeter polystyrene cuvettes for 3 min (UV/VIS spectrophotometer Shimadzu, Japan). The effects of 1 mmol L-1 NaF in the presence of 20 pmol L 1 A1C13 were measured. Data are expressed in percentage of the AChE activity in the absence of aluminum and fluoride ions. No differences between the AChE activity were found between the investigated groups... Table 1. The effect of 1 mM NaF + 20 pM A1C13 on the acetylcholinesterase activity (AChE) in freshly prepared intact RBC and in hemolysate of patients with AD (mean age 72.5 5.1 years), age-matched healthy controls (AM-HS) (72.1 1.6 years), and the group of young healthy subjects (YS) (35.9 8.5 years). Whole venous blood samples were drawn from each subject after overnight fasting., always at 07 30 AM. Red blood cells (RBC) were isolated from the blood of patients with AD, AM-HS, and YS by centrifugation [68], RBC AChE activity was evaluated in intact freshly prepared RBC or hemolyzate following the spectrophotometric method [45] with modifications. Buffer was Tris-HCl, pH 7.5 in the solution of 154 mmol L 1 NaCl, acetylthiocholine iodide was a substrate. Measurement of enzymatic activity was performed in fluorimeter polystyrene cuvettes for 3 min (UV/VIS spectrophotometer Shimadzu, Japan). The effects of 1 mmol L-1 NaF in the presence of 20 pmol L 1 A1C13 were measured. Data are expressed in percentage of the AChE activity in the absence of aluminum and fluoride ions. No differences between the AChE activity were found between the investigated groups...
Fig. 21.9 Room temperature Raman spectra of four BaTiOs ultrathin films on SrTi03 substrates compared to the spectrum of a bare substrate. Arrows mark the phonon peaks of the BaTiOs films. The inset shows Raman spectra of 1.6-nm-thick BaTi03 film and SrTi03 substrate measured at 10 K, and the difference between the two spectra (After Tenne et al. [48])... Fig. 21.9 Room temperature Raman spectra of four BaTiOs ultrathin films on SrTi03 substrates compared to the spectrum of a bare substrate. Arrows mark the phonon peaks of the BaTiOs films. The inset shows Raman spectra of 1.6-nm-thick BaTi03 film and SrTi03 substrate measured at 10 K, and the difference between the two spectra (After Tenne et al. [48])...
Fig. 26. Polarization curves for O2 generation on various metal oxides produced by thermal decomposition of their salts on a titanium substrate. Measurements were recorded with increasing current density in 4 M K.OH at 22°C (266). Fig. 26. Polarization curves for O2 generation on various metal oxides produced by thermal decomposition of their salts on a titanium substrate. Measurements were recorded with increasing current density in 4 M K.OH at 22°C (266).
Fig. 5. Characteristics of thallium cuprate TlCuO(OH) electrosynthesized by anodic electrocrystallization [348] (a) structure calculated on the basis of X-ray crystal analysis (b) resistivity vs. temperature of the deposit on a copper substrate measured by the two-probe technique. Fig. 5. Characteristics of thallium cuprate TlCuO(OH) electrosynthesized by anodic electrocrystallization [348] (a) structure calculated on the basis of X-ray crystal analysis (b) resistivity vs. temperature of the deposit on a copper substrate measured by the two-probe technique.
With most enzymes in DET, with the main exception of peroxidases, substrate measurements can be made only in the range of 10 -10 M. This restriction is due to a kinetic limitation of the heterogeneous electron transfer which can be overcome by engineering specific attachment regions and electron transfer bridges. [Pg.322]

Detailed ICR analysis of the complex reaction pattern induced by the attack of the ions from biacetyl (acetyl, biacetyl, and triacetyl ions) on pyrrole has allowed the demonstration of single and double resonance effects on the abundance of the product ions (72JA6862 73IJM195). Interestingly, triacetyl cations have been found to be more reactive than biacetyl ions toward pyrrole (rate constants 11 versus 4.3 x 10 ° cm molecule sec ), whereas acetyl cations appear unreactive. Furthermore, the rate of the gas-phase reaction of biacetyl cations with pyrrole is only four times as fast as with benzene, in striking contrast with the enormous reactivity difference of the two aromatic substrates measured for a number of electrophilic reactants in solution. [Pg.89]

In the authors judgment, catalytic action in the strict sense of the term, implying regeneration of the catalyst, has been rigorously proven in two cases. With other reactions, however, true catalysis has not been unequivocally established. Michaelis-Menten kinetics, indicative of the formation of a substrate-polymer complex, has been shown with each type of reaction. Some of the activities have been very weak, with reaction times for incomplete conversion of substrate measured in days. Others, although not as rapid as enzyme-catalyzed rates, are relatively fast, e.g., the catalytic decarboxylation of OAA by equimolar amounts of lysine residue in polymeric form was over 90% complete in less than 1 hour. [Pg.409]

For gel purification, 20CM-00 pmol of 32P-labeled RNA crude mixture is mixed as a tracer with 40,000 pmol of unlabeled crude substrate. Measure the radioactivity of a small aliquot of the mixture in a scintillation counter to calculate the specific activity of the RNA. The dsRNA and ssRNA in the crude mix are separated by electrophoresis in a preparative 8% polyacrylamide gel. After visualization by autoradiography, the region of the acrylamide gel containing the dsRNA is excised with a razor blade and the RNA is extracted from the gel. After gel purification, the dsRNA substrate is suspended in buffer I, and the radioactivity of an aliquot is measured on the scintillation counter. From the specific activity of the dsRNA, the amount of gel-extracted substrate can be determined. This is called the cold substrate because the specific activity is lower than that of the hot substrate, which is freshly labeled with 33P for use in the assay. Since a small amount of the purified dsRNA is labeled with 32P, aliquots of gel-purified cold substrate should be stored in an acrylic (3-radiation storage container until they the radiation has decayed with time. [Pg.107]


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