Author
Charles J. Bardawill
Bio: Charles J. Bardawill is an academic researcher from University of Toronto. The author has contributed to research in topics: Blood serum & Reagent. The author has an hindex of 1, co-authored 1 publications receiving 15297 citations.
Topics: Blood serum, Reagent, Biuret test
Papers
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TL;DR: An investigation of the biochemical changes following experimental liver injury felt the need of a simple, rapid, and accurate method for determining the protein fractions in small amounts of serum and began with Kingsley’s biuret procedure.
15,717 citations
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TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
225,085 citations
TL;DR: Using this method, the liped peroxide level in the liver of rats suffering from carbon tetrachloride intoxication was investigated and was in good agreement with previously reported data obtained by measuring diene content.
24,847 citations
TL;DR: This new method maintains the high sensitivity and low protein-to-protein variation associated with the Lowry technique and demonstrates a greater tolerance of the bicinchoninate reagent toward such commonly encountered interferences as nonionic detergents and simple buffer salts.
20,907 citations
TL;DR: The relatively low density of the lipoproteins was utilized by Lindgren, Elliott, and Gofman to separate them from the other serum proteins by ultracentrifugal flotation, and quantitation was subsequently performed by refractometric methods in the analytical ultracentRifuge.
Abstract: In the past few years several methods have been developed for the analysis of serum lipoproteins Lindgren, Elliott, and Gofman (1) have utilized the relatively low density of the lipoproteins to separate them from the other serum proteins by ultracentrifugal flotation Quantitation was subsequently performed by refractometric methods in the analytical ultracentrifuge Separations of lipoproteins have also been made by Cohn fractionation in cold ethanol, and the quantities of lipoprotein have been estimated from the lipid content of the fractions (2, 3) Widely used at the present time is the method of zone electrophoresis with quantitation either by staining (4) or by chemical analysis of eluates from the support
8,544 citations
TL;DR: The turbidity produced when protein is mixed with low concentrations of any of the common protein precipitants can be used as an index of protein concentration, and this advantage is used to eliminate the interference of nucleic acids in the estimation of protein.
Abstract: Publisher Summary The turbidity produced when protein is mixed with low concentrations of any of the common protein precipitants can be used as an index of protein concentration. The resulting turbidity is maximum after about 10 minutes and may be measured spectrophotometrically in the wavelength region of 600 m. Standardization may be effected by comparison with the turbidity produced by a suspension of a dried protein precipitate, or reference may be had to the methyl acrylate-styrene polymer. Turbidimetric techniques are rapid and convenient, but they yield different values with different proteins. They do not permit differentiation between protein and acid-insoluble compounds such as nucleic acids. Protein estimation with the Folin-Ciocalteu reagent include (1) biuret reaction of protein with copper ion in alkali, and (2) reduction of the phosphomolybdic-phosphotungstic reagent by the tyrosine and tryptophan present in the treated protein. Protein estimation by ultraviolet absorption takes advantage of the fact that nucleic acid, however, absorbs much more strongly at 260 mμ than at 280 mμ, whereas with protein the reverse is true. This advantage is used to eliminate, by calculation, the interference of nucleic acids in the estimation of protein.
3,391 citations