http://hoffman.cm.utexas.edu/courses/bradford_assay.pdf

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction

Measurement of protein using bicinchoninic acid

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

/pdf/the-distribution-and-chemical-composition-of-8laba0f2da.pdf

The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum

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.

Spectrophotometric and turbidimetric methods for measuring proteins

http://process.persiangig.com/BioBase/Determination%20of%20Serum%20Proteins%20by%20Means%20of%20the%20BIURET%20Reaction.pdf

Charles J. Bardawill

Papers

Determination of serum proteins by means of the biuret reaction.