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  2. MBAS assay - Wikipedia

    en.wikipedia.org/wiki/MBAS_assay

    A methylene blue active substances assay, or MBAS assay, is a colorimetric analysis test method that uses methylene blue to detect the presence of anionic surfactants (such as a detergent or foaming agent) in a sample of water. An anionic surfactant detected by the color reaction is called a methylene blue active substance (MBAS). [1]

  3. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    After 5 minutes of incubation, the absorbance can be read at 595 nm using a spectrophotometer or a mobile smartphone camera (RGBradford method). [9] This assay is one of the fastest assays performed on proteins. [12] The total time it takes to set up and complete the assay is under 30 minutes. [13] The entire experiment is done at room temperature.

  4. Colorimetric analysis - Wikipedia

    en.wikipedia.org/wiki/Colorimetric_analysis

    Colorimetric analysis is a method of determining the concentration of a chemical element or chemical compound in a solution with the aid of a color reagent.It is applicable to both organic compounds and inorganic compounds and may be used with or without an enzymatic stage.

  5. Colorimetry (chemical method) - Wikipedia

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

    A colorimeter is a device used to test the concentration of a solution by measuring its absorbance of a specific wavelength of light. To use this device, different solutions must be made, and a control (usually a mixture of distilled water and another solution) is first filled into a cuvette and placed inside a colorimeter to calibrate the machine.

  6. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    The methods in this section are primarily computational although they typically require data generated by wet lab experiments. Protein–protein docking , the prediction of protein–protein interactions based only on the three-dimensional protein structures from X-ray diffraction of protein crystals might not be satisfactory.

  7. Karl Fischer titration - Wikipedia

    en.wikipedia.org/wiki/Karl_Fischer_titration

    Although KF is a destructive analysis, the sample quantity is small and is typically limited by the accuracy of weighing. For example, in order to obtain an accuracy of 1% using a scale with the typical accuracy of 0.2 mg, the sample must contain 20 mg water, which is e.g. 200 mg for a sample with 10% water.

  8. 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).

  9. Kjeldahl method - Wikipedia

    en.wikipedia.org/wiki/Kjeldahl_method

    The Kjeldahl method or Kjeldahl digestion (Danish pronunciation: [ˈkʰelˌtɛˀl]) in analytical chemistry is a method for the quantitative determination of a sample's organic nitrogen plus ammonia/ammonium (NH 3 /NH 4 +). Without modification, other forms of inorganic nitrogen, for instance nitrate, are not included in this measurement.