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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 ...
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.
In wine tasting, humans are least sensitive to the taste of sweetness (in contrast to sensitivity to bitterness or sourness) with the majority of the population being able to detect sugar or "sweetness" in wines between 1% and 2.5% residual sugar. Additionally, other components of wine such as acidity and tannins can mask the perception of ...
Proteins are present in wine. The most common proteins include thaumatin-like proteins and chitinases and have a role in the formation of turbidity (haze) [1] especially visible in white wine. [2] The quantity of haze forming is dependent on the quantity of phenolics in the wine. [3] Some of those proteins are considered nuisance.
The binding interaction results in a spectrum shift, enabling quantitative measurement of the protein concentration. A similar colorimetric assay, the Bicinchoninic acid assay, uses a chemical reaction to determine protein concentration. The Biuret assay utilizes a biuret reagent which turns purple in the presence of proteins due to the ...
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
Buffers, such as Tris and ammonia interfere with this assay, therefore rendering this assay inappropriate for protein samples purified from ammonium sulfate precipitation. Due to its insensitivity and little interference by free amino acids, this assay is most useful for whole tissue samples and other sources with high protein concentration. [5]
This method is able to detect as low as 25 μg/ml and up to 2000 μg/ml of protein in a 65 ul sample, using standard protocol. This method may be preferred for samples containing detergents or other reducing agents. This method has a fast detection speed and low protein-to-protein variability in comparison to the BCA or Coomassie (Bradford ...
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