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  2. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    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.

  3. Protein methods - Wikipedia

    en.wikipedia.org/wiki/Protein_methods

    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.

  4. Marion M. Bradford - Wikipedia

    en.wikipedia.org/wiki/Marion_M._Bradford

    Marion Mckinley Bradford (October 28, 1946 - May 3, 2021) was an American scientist [1] who developed and patented the Bradford protein assay, [2] a method to quickly quantify the amount of protein in a sample. [3] [4] His paper describing the method is among the most cited scholarly articles of all time. [5] [6] [7]

  5. Coomassie brilliant blue - Wikipedia

    en.wikipedia.org/wiki/Coomassie_brilliant_blue

    The Bradford assay uses the spectral properties of Coomassie brilliant blue G-250 to estimate the amount of protein in a solution. [19] A protein sample is added to a solution of the dye in phosphoric acid and ethanol. Under the acid conditions the dye is normally a brownish colour but on binding to the protein the blue form of the dye is produced.

  6. Molecular biology - Wikipedia

    en.wikipedia.org/wiki/Molecular_biology

    This method was developed in 1975 by Marion M. Bradford, and has enabled significantly faster, more accurate protein quantitation compared to previous methods: the Lowry procedure and the biuret assay. [41] Unlike the previous methods, the Bradford assay is not susceptible to interference by several non-protein molecules, including ethanol ...

  7. Bicinchoninic acid assay - Wikipedia

    en.wikipedia.org/wiki/Bicinchoninic_acid_assay

    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 ...

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  9. Quantitative proteomics - Wikipedia

    en.wikipedia.org/wiki/Quantitative_proteomics

    The concentration of a certain protein in a sample may be determined using spectrophotometric procedures. [5] The concentration of a protein can be determined by measuring the OD at 280 nm on a spectrophotometer, which can be used with a standard curve assay to quantify the presence of tryptophan, tyrosine, and phenylalanine. [6]