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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 was born October 28, 1946, in Rome, Georgia, US, and received his B.A. from Shorter College there in 1967. [1] In 1971 he married Janet Holliday. [1] [8] He obtained his Ph.D. in biochemistry from the University of Georgia in 1975, and his use of the Coomassie Brilliant Blue G-250 dye to detect proteins, which became known as the Bradford assay, was patented in 1976.
The Bradford assay is a molecular biology technique which enables the fast, accurate quantitation of protein molecules utilizing the unique properties of a dye called Coomassie Brilliant Blue G-250. [41] Coomassie Blue undergoes a visible color shift from reddish-brown to bright blue upon binding to protein. [41]
Several reliable methods for quantifying protein have been developed to simplify the process. These methods include Warburg–Christian method, Lowry assay, and Bradford assay (all of which rely on absorbance properties of macromolecules). Bradford assay method uses a dye to bind to protein. Most commonly, Coomassie brilliant blue G-250 dye is ...
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The ability of the Coomassie dye to target amino acids with aromatic groups (phenylalanine, tyrosine, tryptophan) and basic side chains (lysine, arginine and histidine) allows the Bradford assay to be used for fingerprint analysis. The assay was successfully used to identify the biological sex of the fingerprint. Female samples were shown to ...
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