Showing papers on "Bradford protein assay published in 1992"
TL;DR: In this study, lipoprotein protein values obtained by the BCA method were compared to a standard modification of the Lowry et al. procedure, and the standard BCA assay was found to overestimate the protein content of very low density lipop Protein by approximately 70% and low density Lipoprotein by approximately 30%; high density lipobrotein values compared favorably.
159 citations
TL;DR: An assay was based on reaction of free e-amino groups in proteins with the o-phthalaldehyde/N-acetyl-L-cysteine reagent to form isoindoles, which absorb at 335 nm and was simpler and more convenient than other methods, since it did not require hydrolysis, amino acid analysis, long heating periods or solvent extraction.
Abstract: An assay was based on reaction of free e-amino groups in proteins with the o-phthalaldehyde/N-acetyl-L-cysteine reagent to form isoindoles, which absorb at 335 nm. The procedure was suitable for proteins or mixtures of proteins with available lysine contents of more than 5 moles lysine/mole protein and required absence of free amino acids and peptides. This method was simpler and more convenient than other methods, since it did not require hydrolysis, amino acid analysis, long heating periods or solvent extraction.
37 citations
TL;DR: The results have suggested this TCA/SDS precipitation method to be useful for quantitating dilute protein samples containing high concentrations of detergents and other reagents commonly employed in studying membrane proteins.
31 citations
TL;DR: The solubility of the protein-Coomassie brilliant blue (CBB) complex formed upon Bradford (Anal. Biochem. 79, 544-552, 1977) protein assay has been investigated and results show complete loss of color yield in the respective supernates and filtrates.
30 citations
TL;DR: The principle of the protein assay is presented as a model that can be used to formulate protein assays of desired specification that is stable and rapid without a buffering agent in alkaline copper solution.
30 citations
Journal Article•
TL;DR: In this article, protein was estimated from common pollen and fungal antigens by modified Lowry's (ML), Bradford (B), micro-Kjeldahl (MK), Bicinchoninic acid (BCA), and modified BCA (MBCA) assays.
Abstract: The usual procedures available for protein estimation of biological extracts often give variable results due to presence of many peptides and coloured materials. To identify a suitable method for allergenic extracts, protein was estimated from common pollen and fungal antigens by modified Lowry's (ML), Bradford (B), micro-Kjeldahl (MK), Bicinchoninic acid (BCA) and modified BCA (MBCA) assays. Bradford assay resulted in low protein values, whereas BCA method gave very high values in general. Statistical analysis of the results revealed similarity between protein values quantitated by MK, ML and MBCA methods for most of the extracts. Graded volumes of the extracts on subjecting to protein estimation by these three methods showed linear response, while recovery of a protein (bovine serum albumin) added to the extracts was greater than 90%.
25 citations
TL;DR: In this article, trichloroacetic acid (TCA; 5%) was found to release iron quantitatively from a number of ferrocene derivatives, and free iron was then determined spectrophotometrically, using 564 nm absorbance maximum of the Fe(ferrozine) 2+ 3 complex.
12 citations
TL;DR: The method allows simultaneous protein assay and recovery of microgram amounts of protein from dilute solution and could be widely applied for conserving, concentrating and desalting minute amounts of valuable sample prior to electrophoretic analysis.
Abstract: The interaction of protein with Coomassie Brilliant Blue G-250 results in formation of an insoluble protein-dye complex which can be recovered by centrifugation and redissolved for electrophoretic analysis. The precipitated protein can be washed in acetone to remove excess dye in order to enhance resolution. The residual dye becomes dissociated from the proteins on electrophoresis and can be exploited as a "dye front". The method allows simultaneous protein assay and recovery of microgram amounts of protein from dilute solution and could be widely applied for conserving, concentrating and desalting minute amounts of valuable sample prior to electrophoretic analysis.
10 citations
9 citations
5 citations
TL;DR: The Coomassie brilliant blue assay for the determination of protein has been extended to rapidly and conveniently measure the protein concentration of cells growing in culture in a 96-well microtiter format.
Journal Article•
TL;DR: A Ponceau S reagent with high stability and slight response to pH changes, presence of organic solvents and detergents was prepared and tested to be suitable to quantify, in one-step procedure, different standard proteins.
Abstract: A Ponceau S reagent with high stability and slight response to pH changes, presence of organic solvents and detergents was prepared. Under these conditions, the reagent was tested to be suitable to quantify, in one-step procedure, different standard proteins. Moreover, this method offers the possibility to measure the protein content in the presence of the detergent Triton X-100.