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Polyacrylamide, determination

Plutonium, determination of 154-157 Polyacrylamide, determination of 217 Polyaromatic hydrocarbons, determination of 110-112,127-133,... [Pg.493]

Before polyacrylamides are sold, the amount of residual acrylamide is determined. In one method, the monomer is extracted from the polymer and the acrylamide content is determined by hplc (153). A second method is based on analysis by cationic exchange chromatography (154). For dry products the particle si2e distribution can be quickly determined by use of a shaker and a series of test sieves. Batches with small particles can present a dust ha2ard. The percentage of insoluble material is determined in both dry and emulsion products. [Pg.144]

Polyacrylamide, whether charged or not, can be detected by reactions of the amide group (67,68) however, a number of substances can interfere with the determination. If the molecular weight is high enough, flocculation of a standard slurry of clay or other substrate is a sensitive method for detecting low levels of polyacrylamide (69). Once polymers are adsorbed on a surface, many of these methods caimot be used. One exception is the use of a labeled polymer. [Pg.36]

In semi-cristalline polymers, rate-enhancement under stress has been frequently observed, e.g. in UV-photooxidation of Kapron, natural silk [80], polycaprolactam and polyethylene terephthalate [81]. Quantitative interpretation is, however, difficult in these systems although the overall rate is determined by the level of applied stress, other stress-dependent factors like the rate of oxygen diffusion or change in polymer morphology could occur concurrently and supersede the elementary molecular steps [82, 83], Similar experiments in the fluid state showed unequivocally that flow-induced stresses can accelerate several types of reactions, the best studied being the hydrolysis of DNA [84] and of polyacrylamide [85]. In these examples, hydrolysis involves breaking of the ester O —PO and the amide N —CO bonds. The tensile stress stretches the chain, and therefore, facilitates the... [Pg.105]

In the same year, Fulda and Tieke [75] reported on Langmuir films of monodisperse, 0.5-pm spherical polymer particles with hydrophobic polystyrene cores and hydrophilic shells containing polyacrylic acid or polyacrylamide. Measurement of ir-A curves and scanning electron microscopy (SEM) were used to determine the structure of the monolayers. In subsequent work, Fulda et al. [76] studied a variety of particles with different hydrophilic shells for their ability to form Langmuir films. Fulda and Tieke [77] investigated the influence of subphase conditions (pH, ionic strength) on monolayer formation of cationic and anionic particles as well as the structure of films made from bidisperse mixtures of anionic latex particles. [Pg.217]

Molecular weight determination The molecular weight of the purified enzyme was determined by both gel filtration chromatograph and SDS polyacrylamide gel electrophoresis (16). Toyopearl 55HW gel (Toyo SF 160K, Toyo, Co.,Ltd., Tokyo) was used for gel filtration and 0.05 N acetate buffer pH 5.25 was used as buffer. [Pg.717]

Figures 6, 7 and 9 show calibration curves using two multi-column combinations and illustrate the degree of "optimization obtained in this system. The mobile phases for Figures 6 and 7 contained 0.025 g polyethylene oxide and ion exclusion and adsorption effects should therefore be largely eliminated. Figure 6 shows that reasonably good resolution can be obtained with a combination of five columns but does exhibit some loss of peak separation at the low cuid high MW ends. In Figure 7 the effect of adding a sixth column of small pore size is illustrated and it is seen that resolution at the low MW end is thereby somewhat improved. This calibration curve is effectively linear with a change of slope at 500,000 MW. It should provide a useful aqueous GPC system for MW and MWD determination of nonionic polyacrylamides. Figures 6, 7 and 9 show calibration curves using two multi-column combinations and illustrate the degree of "optimization obtained in this system. The mobile phases for Figures 6 and 7 contained 0.025 g polyethylene oxide and ion exclusion and adsorption effects should therefore be largely eliminated. Figure 6 shows that reasonably good resolution can be obtained with a combination of five columns but does exhibit some loss of peak separation at the low cuid high MW ends. In Figure 7 the effect of adding a sixth column of small pore size is illustrated and it is seen that resolution at the low MW end is thereby somewhat improved. This calibration curve is effectively linear with a change of slope at 500,000 MW. It should provide a useful aqueous GPC system for MW and MWD determination of nonionic polyacrylamides.
Fig. 4. Critical concentrations of polystyrene/toluene and polyacrylamide/water at 25 °C in relation to molar mass determined by viscometry and light scattering... [Pg.13]

In the previously described electrophoretic methods, the capillary was filled with electrolytes only. Another mode of operation in capillary electrophoresis involves filling the capillary with gel or viscous polymer solutions. If desired, a column can be packed with particles and equipped with a frit.68 This mode of analysis has been favorably used for the size determination of biologically important polymers, such as DNA, proteins, and polysaccharides. The most frequently used polymers in capillary gel electrophoresis are cross-linked or linear polyacrylamide,69 cellulose derivatives,70-75 agarose,76 78 and polyethylene glycols. [Pg.400]

Figure 5.11. Generic approaches to identify interacting proteins within complexes. The complex is isolated from cells by affinity purification using a tag sequence attached to a protein known to be in the complex. Alternatively, the complex can be immunprecipitated with an antibody to one of the proteins in the complex. The proteins are resolved by polyacrylamide gel electrophoresis, proteolyzed, and the mass of the resulting peptides is determined by mass spectrometry. Alternatively, the proteins can be proteolyzed and the resulting peptides resolved by liquid chromatography. The peptide masses are then determined by mass spectrometry and used for database searching to identify the component proteins. Figure 5.11. Generic approaches to identify interacting proteins within complexes. The complex is isolated from cells by affinity purification using a tag sequence attached to a protein known to be in the complex. Alternatively, the complex can be immunprecipitated with an antibody to one of the proteins in the complex. The proteins are resolved by polyacrylamide gel electrophoresis, proteolyzed, and the mass of the resulting peptides is determined by mass spectrometry. Alternatively, the proteins can be proteolyzed and the resulting peptides resolved by liquid chromatography. The peptide masses are then determined by mass spectrometry and used for database searching to identify the component proteins.
This study aims at determining the effects of calcium on the adsorption of polyacrylamides and xanthans on siliceous minerals and kaolinite. [Pg.228]


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See also in sourсe #XX -- [ Pg.217 ]

See also in sourсe #XX -- [ Pg.82 , Pg.215 ]




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