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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. It is named for the biochemist Oliver H. Lowry who developed the reagent in the 1940s. His 1951 paper describing the technique is the most-highly cited paper ever ...
This reagent is part of the Lowry protein assay, and will also react with some nitrogen-containing compounds such as hydroxylamine and guanidine. [3] The reagent has also been shown to be reactive towards thiols, many vitamins, the nucleotide base guanine , the trioses glyceraldehyde and dihydroxyacetone , and some inorganic ions.
Bradford protein assay: Detection in the range of ~1 mg/mL; Biuret Test Derived Assays: Bicinchoninic acid assay (BCA assay): Detection down to 0.5 μg/mL; Lowry Protein assay: Detection in the range of 0.01–1.0 mg/mL; Fluorescamine: Quantifies proteins and peptides in solution if primary amine are present in the amino acids
As of September 2015, his 1951 paper in the Journal of Biological Chemistry [5] describing the protein assay was still the most-highly cited paper in history, with more than 310,000 citations, [6] although Lowry stated it was not the most important paper he had ever written.
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.
An assay (analysis) is never an isolated process, as it must be accompanied with pre- and post-analytic procedures. Both the communication order (the request to perform an assay plus related information) and the handling of the specimen itself (the collecting, documenting, transporting, and processing done before beginning the assay) are pre-analytic steps.
Additionally, the BCA protein assay gives the important benefit of compatibility with substances such as up to 5% surfactants in protein samples. In the Lowry protein assay, Cu + is oxidized back to Cu 2+ by Mo VI in the Folin–Ciocalteu reagent, which forms molybdenum blue (Mo IV).
The Lowry method is sensitive to protein concentrations as low as 20 ug/mL. The disadvantage of this method is the long incubation time and there are often interferences with commonly used buffers. This method is also subject to protein-to-protein variation due to the correlation of colour intensity dependent on the content of tyrosine and ...