2005
DOI: 10.1590/s1516-89132005000300008
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Spectrophotometric determination of total proteins in blood plasma: a comparative study among dye-binding methods

Abstract: A comparative study between the biuret method (standard method for total proteins) and spectrophotometric methods using dyes (Bradford, 3',3'',5',

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Cited by 37 publications
(28 citation statements)
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“…It may be performed also in microtitre plates using micro volumes, but its application area is mainly restricted to research laboratories (Da Silva and Zezzi Arruda 2006). Unfortunately, the Bradford assay is only linear over a short range (to 2000 µg/ml) and shows a curvature over this range of protein concentration, which necessitates the dilution of samples before further analysis (Zor and Selinger 1996;Zaia et al 2005).…”
Section: Total Proteinmentioning
confidence: 99%
“…It may be performed also in microtitre plates using micro volumes, but its application area is mainly restricted to research laboratories (Da Silva and Zezzi Arruda 2006). Unfortunately, the Bradford assay is only linear over a short range (to 2000 µg/ml) and shows a curvature over this range of protein concentration, which necessitates the dilution of samples before further analysis (Zor and Selinger 1996;Zaia et al 2005).…”
Section: Total Proteinmentioning
confidence: 99%
“…A highly sensitive flow injection method was proposed for the determination of proteins using Coomassie Brilliant Blue G-250 (CBB) [13]. Zaia et al found that total protein obtained by using the Bradford method was not statistically different (p > 0.05) from the results obtained by the Biuret standard method [14]. However, a short linear range for the calibration graph was offered by this method.…”
Section: Introductionmentioning
confidence: 99%
“…However, the method still failed when trying to separate the glycoforms of each glycopeptide, due to the use of a C18 column. CE has been described as an excellent analytical technique for the separation of glycopeptide glycoforms, which vary in the composition of the monosaccharides, especially if they differ in the number of sialic acids . In the previous work, we evaluated CE‐MS for the separation of Tf glycopeptide glycoforms, but the surfactant seemed to interfere with the inner surface of the silica capillary walls, provoking a distortion of the electrophoretic peaks, which were much wider than expected for a glycopeptide or a peptide .…”
Section: Resultsmentioning
confidence: 99%
“…Additionally, the recent development of novel nano‐ESI sheathless interfaces is revitalizing the interest in CE‐MS as a high‐separation efficiency . Several authors have demonstrated the excellent performance of CE‐MS for the analysis of glycopeptides from glycoprotein digests , largely due to the fact that the different glycopeptide glycoforms are easily separated in CE‐MS, especially if the number of sialic acids is different. Moreover, the reagent consumption is greatly reduced and the analysis time is pretty low.…”
Section: Introductionmentioning
confidence: 99%