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Glutathione assays

Methods of Glutathione Assay—A Review of Classical Methods... [Pg.63]

In order to determine the methods of glutathione assay currently in use, a survey was made of the literature during the five-year period between 1948 and 1952. During this period approximately 300 papers on glutathione were published. It was possible to obtain about two thirds of these for study. Over half of the papers described the use of glutathione and were not concerned with assay. Glutathione determinations were made in 85 cases (Fig. 1). The iodometric titration method was used in almost half... [Pg.63]

The glutathione (GSH) level was assayed by the method of Sedlak and Lindsay (ref. 14), using Ellman s reagent (5,5-dithio-bis-(2-nitrobenzoic acid). Calibration was carried out parallely to each series, using reduced glutathione as a standard. [Pg.390]

M26. Miwa, S., Luzzatto, L., Rosa, R., Paglia, D. E., Schroter, W De Flora, A., Fujii, H., Board, P. G and Beutler, E., International Committee for Standardization in Haematology Recommended methods for an additional red cell enzyme (pyrimidine 5 -nucleotidase) assay and the determination of red cell adenosine 5 -triphosphate, 2,3-diphosphoglycerate and reduced glutathione. Clin. Lab. Haematol. 11, 131-138 (1989). [Pg.47]

Figure 7.6. Purification of protein from pooled yeast strains. Each yeast ORF was cloned as a fusion to glutathione-S-transferase in a protein expression vector to create 6144 yeast strains. The individual strains were pooled in groups of 96 to create a set of 64 pools. Each pool was grown and the 96 fusion proteins are purified in batch. Each pool was then assayed for a biochemical function (Martzen et al., 1999). Pools positive for function were then deconvoluted using smaller pools consisting of strains from rows and columns of a 96-well plate. Figure 7.6. Purification of protein from pooled yeast strains. Each yeast ORF was cloned as a fusion to glutathione-S-transferase in a protein expression vector to create 6144 yeast strains. The individual strains were pooled in groups of 96 to create a set of 64 pools. Each pool was grown and the 96 fusion proteins are purified in batch. Each pool was then assayed for a biochemical function (Martzen et al., 1999). Pools positive for function were then deconvoluted using smaller pools consisting of strains from rows and columns of a 96-well plate.
Glutathione semiquantitative assay in small volume of samples 157... [Pg.263]

In these situations, biological activity will be reduced for reactive substrates that are consumed intracellularly or in a biological assay. In the case of TV-acyloxy-TV-alkoxyamides, those mutagens that are less prone to solvolysis or reaction with adventitious nucleophiles such as glutathione, will be present at higher concentrations at DNA, the intracellular target. [Pg.105]

A colorimetric assay for lecithin and choline was described by Kotsira and Klonis (1998) using two enzymes (phospholipase and choline oxidase) and an indicator dye conjugate (bromothymol blue-glutathione) co-immobilised on a glutaraldehyde-activated polyacrylamide transparent gel. The change of the... [Pg.130]


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See also in sourсe #XX -- [ Pg.393 ]




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