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The Bradford protein assay (also known as the Coomassie protein assay) was developed by Marion M. Bradford in 1976. [1] It is a quick and accurate [2] spectroscopic analytical procedure used to measure the concentration of protein in a solution. The reaction is dependent on the amino acid composition of the measured proteins.
Bradford assay method uses a dye to bind to protein. Most commonly, Coomassie brilliant blue G-250 dye is used. When free of protein, the dye is red but once bound to protein it turns blue. [11] The dye-protein complex absorbs light maximally at the wavelength 595 nanometers and is sensitive for samples containing anywhere from 1 ug to 60 ug.
The Lowry protein assay is a biochemical assay for determining the total level of protein in a solution. The total protein concentration is exhibited by a color change of the sample solution in proportion to protein concentration, which can then be measured using colorimetric techniques .
The Dumas technique has been automated and instrumentalized, so that it is capable of rapidly measuring the crude protein concentration of food samples. This automatic Dumas technique has replaced the Kjeldahl method as the standard method of analysis for nutritional labelling of protein content of foods (except in high fat content foods where ...
BCA protein assay in a 96 well plate. The bicinchoninic acid assay (BCA assay), also known as the Smith assay, after its inventor, Paul K. Smith at the Pierce Chemical Company, [1] now part of Thermo Fisher Scientific, is a biochemical assay for determining the total concentration of protein in a solution (0.5 μg/mL to 1.5 mg/mL), similar to Lowry protein assay, Bradford protein assay or ...
A tri- or tetra-dentate chelation with the peptide nitrogen produces the characteristic color. This is found with dipeptides. [8] The reagent is commonly used in the biuret protein assay, a colorimetric test used to determine protein concentration by UV/VIS spectroscopy at wavelength 540 nm.
The Warburg–Christian method is an ultraviolet spectroscopic protein and nucleic acid assay method based on the absorbance of UV light at 260 nm and 280 nm wavelengths. Proteins generally absorb light at 280 nanometers due to the presence of tryptophan and tyrosine. Nucleic acids absorb more at 260 nm, primarily due to purine and pyrimidine ...
The classic assays for protein concentration in food are the Kjeldahl method and the Dumas method. These tests determine the total nitrogen in a sample. The only major component of most food which contains nitrogen is protein (fat, carbohydrate and dietary fiber do not contain nitrogen).
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