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  2. Biuret test - Wikipedia

    en.wikipedia.org/wiki/Biuret_test

    The characteristic color of a positive biuret test. In chemistry, the biuret test (IPA: / ˌ b aɪ j ə ˈ r ɛ t /, / ˈ b aɪ j ə ˌ r ɛ t / [1]), also known as Piotrowski's test, is a chemical test used for detecting the presence of at least two peptide bonds in a molecule.

  3. Colorimetry (chemical method) - Wikipedia

    en.wikipedia.org/wiki/Colorimetry_(chemical_method)

    Colorimetric assays use reagents that undergo a measurable color change in the presence of the analyte. They are widely used in biochemistry to test for the presence of enzymes, specific compounds, antibodies, hormones and many more analytes. For example, para-Nitrophenylphosphate is converted into a yellow product by alkaline phosphatase enzyme.

  4. Xanthoproteic reaction - Wikipedia

    en.wikipedia.org/wiki/Xanthoproteic_reaction

    If the test is positive the proof is neutralized with an alkali, turning dark yellow. The yellow colour is due to xanthoproteic acid which is formed due to nitration of certain amino acids, most common examples being tyrosine and tryptophan. [1] This chemical reaction is a qualitative test, determining the presence or absence of proteins.

  5. Lowry protein assay - Wikipedia

    en.wikipedia.org/wiki/Lowry_protein_assay

    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).

  6. Bicinchoninic acid assay - Wikipedia

    en.wikipedia.org/wiki/Bicinchoninic_acid_assay

    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 ...

  7. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    By using the Bradford protein assay, one can avoid all of these complications by simply mixing the protein samples with the Coomassie brilliant blue G-250 dye (Bradford reagent) and measuring their absorbances at 595 nm, which is in the visible range [8] and may be accurately measured by the use of a mobile smartphone camera. [9]

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  9. Adamkiewicz reaction - Wikipedia

    en.wikipedia.org/wiki/Adamkiewicz_reaction

    The Adamkiewicz reaction is part of a biochemical test used to detect the presence of the amino acid tryptophan in proteins. When concentrated sulfuric acid is combined with a solution of protein and glyoxylic acid, a red/purple colour is produced. It was named after its discoverer, Albert Wojciech Adamkiewicz.