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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.
Identification is only possible with a microbiological culture.API test strips consist of wells containing dehydrated substrates such as the redox substrates, electrogenic substrates and luminogenic substrates to detect enzymatic activity, usually related to the fermentation of carbohydrate or catabolism of proteins or amino acids by the inoculated organisms.
This then allows for biosynthetic or biochemical pathway mapping that can help determine which enzyme or enzymes are mutated and dysfunctional in the auxotrophic strains of bacteria being studied. [2] Researchers have used strains of E. coli auxotrophic for specific amino acids to introduce non-natural amino acid analogues into proteins. For ...
These amino acids are then separated using 2-dimensional thin layer chromatography, along with amino acid standards for the three amino acids that are phosphorylated in eukaryotes: serine, threonine, and tyrosine. These amino acid standards can be visualized on the TLC substrate by exposure to ninhydrin, which colors the amino acids a visible ...
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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M13 filamentous phage containing sequence coding for the first 145 amino acid was later constructed by Messing et al., and α-complementation via the use of a vector was demonstrated by the formation of blue plaques when cells containing the inactive protein were infected by the phage and then grown in plates containing X-gal. [3]
Stable isotope labeling with amino acids in cell culture is a method that involves metabolic incorporation of “heavy” C- or N-labeled amino acids into proteins followed by MS analysis. SILAC requires growing cells in specialized media supplemented with light or heavy forms of essential amino acids, lysine or arginine.
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