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Absorbance matrix creating

We have been considering equations [20] through [22] for the case where we are creating an absorbance matrix, A, that contains only a single spectrum... [Pg.40]

Absorbance matrix, 7,9, 11 creating, 37 Abstract factors, 84 Accuracy... [Pg.201]

Here, R is regarded as the sum of the specific energies absorbed in creating new surfaces in fiber r, matrix Rm and at the interface G based on the nominal transverse area neglecting the cylindrical interface area... [Pg.245]

One of the most important advantages of HPLC over spectrophoto-metric methods lies in its specificity and selectivity due to its separation capability. Through chromatographic separations, the analytes of interest can be detected and quantified without interference from the typical matrix that includes excipients, antioxidants, preservatives, and dissolution media. Ion-pair HPLC was used to monitor the dissolution of pentamidine from EVA sustained-release film where polymeric matrices could create significant bias if a spectrophotometric method were used. Due to their strong UV absorbance, the antioxidants and preservatives (e.g., BHA, BHT, ascorbic acid and propyl gallate) are often the major... [Pg.384]

Instruments that have burners and require nebulisation of dilute aqueous sample solutions generally have low background noise in the signal. With graphite furnaces, incomplete atomisation of the solid sample at elevated temperatures can produce interfering absorptions. This matrix effect does not exist in an isolated state and thus cannot be eliminated by comparison with a reference beam. This is notably the case for solutions containing particles in suspension, ions that cannot be readily reduced and organic molecules, all of which create a constant absorbance in the interval covered by the monochromator. [Pg.264]

Fig. 3. Analysis of peptide-lipid interactions using ProteinChip arrays. Vesicles are absorbed to H50 ProteinChip arrays via interactions with C8 functional groups, creating a supported lipid monolayer on the chip surface (A, B). Samples are applied to the chip, incubated for 5 min (C), and washed to remove nonspecifically bound proteins (D). Matrix is added (E), and the array is introduced into the ProteinChip reader, where the laser is fired onto the chip surface. Peptides retained on the surface are finally resolved by TOF-MS, displaying mass-to-charge versus signal intensity (F, G). (Adapted from ProteinChip technology training course, Bio-Rad Laboratories.)... Fig. 3. Analysis of peptide-lipid interactions using ProteinChip arrays. Vesicles are absorbed to H50 ProteinChip arrays via interactions with C8 functional groups, creating a supported lipid monolayer on the chip surface (A, B). Samples are applied to the chip, incubated for 5 min (C), and washed to remove nonspecifically bound proteins (D). Matrix is added (E), and the array is introduced into the ProteinChip reader, where the laser is fired onto the chip surface. Peptides retained on the surface are finally resolved by TOF-MS, displaying mass-to-charge versus signal intensity (F, G). (Adapted from ProteinChip technology training course, Bio-Rad Laboratories.)...
To uniquely identify the intrinsic feature of the material, one method of sample preparation is to pelletize the explosive powders or crystals [14], It is standard practice in far-infrared (THz) spectroscopy to press samples into pellet form to measure the THz transmission spectra. When the sample is a powder with a grain size comparable to the THz wavelength (about 300 microns), the powder strongly scatters the THz radiation. Another method of sample preparation is to mix the material (e.g., RDX) with an inert matrix or filler material to create a pellet. The filler is typically a material that is transparent in the THz such as polyethylene. This allows dilute concentrations of a highly absorbing agent to be measured. [Pg.328]


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