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Acrylamide gel

At a somewhat more basic level, both agarose and acrylamide gel systems have been used for direct immunofixation. In these gels, samples are electrophoresed and then immunofixed by either using stnps of cellulose acetate soaked in an antibody or the antibody is placed direcdy over the sample area of the gel. [Pg.184]

Raymond, S Weintranb, LS, Acrylamide Gel as a Supporting Medium for Zone Electrophoresis, Science 130, 7111,1959. [Pg.619]

The most spectacular results, in terms of comparison between CFPs- and carbon-supported metal catalysts, were likely provided by Toshima and co-workers [33,34]. As illustrated in Section 3.3.3, they were able to produce platinum and rhodium catalysts by the covalent immobilization of pre-formed, stabilized metal nanoclusters into an amine functionalized acrylamide gel (Scheme 5). To this purpose, the metal nanopartides were stabilized by a linear co-polymer of MMA and VPYR. The reaction between its ester functions and the amine groups of the gel produced the covalent link between the support and the... [Pg.224]

Figure 14 The free volume theory of Yasuda and coworkers holds for the diffusion of acetaminophen in swollen 10 X 4 poly(lV-isopropyl acrylamide) gel. (Adapted from Ref. 176.)... Figure 14 The free volume theory of Yasuda and coworkers holds for the diffusion of acetaminophen in swollen 10 X 4 poly(lV-isopropyl acrylamide) gel. (Adapted from Ref. 176.)...
SH Gehrke, M Palasis, MK Akhtar. Effect of synthesis conditions on properties of polyfALisopropyl acrylamide) gels. Polym Int 29 29-36, 1992. [Pg.546]

The utility of MALDI-FTMS analysis for use in chemotaxonomic applications has been established, but this method can be applied to other areas of interest, such as biomedical and environmental analyses. A common method used by biochemists and biologists today is recombinant overexpression of proteins using bacterial whole cells in cases where large quantity of a protein is desired. The main method presently used to determine if the overexpression was successful is the use of SDS-PAGE (sodium dodecylsulfate-poly acrylamide gel... [Pg.293]

Hydrogen peroxide, Poly(acrylamide) gel, etc. See Hydrogen peroxide 2-Ethoxyethanol, etc. See other PEROXIDISABLE compounds... [Pg.568]

C. Beauchamp and I. Fridovich, Superoxide dismutase. Improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44, 276-287 (1971). [Pg.203]

Preparative electrophoresis on Sephadex G-25 (Ref. 168) or double isoelectric focusing,208 preceded by chromatography on Sephadex G-75, CM-cellulose, and calcium phosphate, was used for the isolation of endo-D-galacturonanase from the filtrate of a Verticillium albo-atrum culture. The homogeneity was confirmed in both cases by electrophoresis on poly(acrylamide) gel. The molecular weight of the enzyme was close to the values found for Aspergillus endo-D-galacturonanases. [Pg.363]

Using an acrylamide-gel as support, Coombe- 0 has demonstrated the quantitative assay of neomycin with a recovery of 96% in the presence of bacitracin and polymixin. In this case quantitation was achieved by densitometry after staining the gel with naphthalene black. [Pg.440]

Acrylamide-based products, in paper manufacture, 18 115 Acrylamide copolymers, functional monomers used in, 11 628 Acrylamide gels, 1 680 Acrylamide graft copolymers, 18 625 Acrylamide polymers, 1 292, 304-333. [Pg.10]

Figure 7.1. Effect of GM-CSF on neutrophil protein biosynthesis. Human neutrophils were incubated in RPMI1640 medium supplemented with 2.5% foetal calf serum and 60 jtCi/ml [35S]-methionine, in the presence and absence of 50 U/ml GM-CSF. After 4 h incubation at 37 °C, the cells were pelleted by low-speed centrifugation. The proteins in the cell pellets were precipitated by 10% trichloracetic acid and then analysed by two-dimensional polyacrylamide gel electrophoresis, using iso-electrofocussing in the first dimension. Electrophoresis in the second dimension was performed in the presence of SDS and used a 12% acrylamide gel. Source Experiment of Becky Stringer. Figure 7.1. Effect of GM-CSF on neutrophil protein biosynthesis. Human neutrophils were incubated in RPMI1640 medium supplemented with 2.5% foetal calf serum and 60 jtCi/ml [35S]-methionine, in the presence and absence of 50 U/ml GM-CSF. After 4 h incubation at 37 °C, the cells were pelleted by low-speed centrifugation. The proteins in the cell pellets were precipitated by 10% trichloracetic acid and then analysed by two-dimensional polyacrylamide gel electrophoresis, using iso-electrofocussing in the first dimension. Electrophoresis in the second dimension was performed in the presence of SDS and used a 12% acrylamide gel. Source Experiment of Becky Stringer.

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See also in sourсe #XX -- [ Pg.48 , Pg.50 , Pg.55 ]

See also in sourсe #XX -- [ Pg.110 ]




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