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The biuret reagent is made of sodium hydroxide (NaOH) and hydrated copper(II) sulfate, together with potassium sodium tartrate, [7] the latter of which is added to chelate and thus stabilize the cupric ions. The reaction of the cupric ions with the nitrogen atoms involved in peptide bonds leads to the displacement of the peptide hydrogen atoms ...
The biuret test is a chemical test for proteins and polypeptides. It is based on the biuret reagent, a blue solution that turns violet upon contact with proteins, or any substance with peptide bonds. The test and reagent do not actually contain biuret; they are so named because both biuret and proteins have the same response to the test.
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 traditional method for measuring total protein uses the biuret reagent, but other chemical methods such as dye-binding and refractometry are now available. The measurement is usually performed on automated analysers along with other laboratory tests.
The method combines the reactions of copper ions with the peptide bonds under alkaline conditions (the Biuret test) with the oxidation of aromatic protein residues. The Lowry method is based on the reaction of Cu +, produced by the oxidation of peptide bonds, with Folin–Ciocalteu reagent (a mixture of phosphotungstic acid and phosphomolybdic acid in the Folin–Ciocalteu reaction).
Benedict's reagent (often called Benedict's qualitative solution or Benedict's solution) is a chemical reagent and complex mixture of sodium carbonate, sodium citrate, and copper(II) sulfate pentahydrate. [1] It is often used in place of Fehling's solution to detect the presence of reducing sugars and other reducing substances. [2]
Lowry assay is similar to biuret assays, but it uses Folin reagent which is more accurate for quantification. Folin reagent is stable at only acidic conditions and the method is susceptible to skewing results depending on how much tryptophan and tyrosine is present in the examined protein. [12]
The dye reagent is a stable ready to use product prepared in phosphoric acid. It can remain at room temperature for up to 2 weeks before it starts to degrade. Protein samples usually contain salts, solvents, buffers, preservatives, reducing agents and metal chelating agents.