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  2. Nucleic acid quantitation - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_quantitation

    For pure DNA, A 260/280 is widely considered ~1.8 but has been argued to translate - due to numeric errors in the original Warburg paper - into a mix of 60% protein and 40% DNA. [6] The ratio for pure RNA A 260/280 is ~2.0. These ratios are commonly used to assess the amount of protein contamination that is left from the nucleic acid isolation ...

  3. Qubit fluorometer - Wikipedia

    en.wikipedia.org/wiki/Qubit_fluorometer

    Upon binding to DNA, the dye molecules assume a more rigid shape and increase in fluorescence by several orders of magnitude, most likely due to intercalation between the bases. [9] [10] The Qubit fluorometer, a device designed to measure fluorescence signals from samples, operates by correlating these signals with known concentrations of probes.

  4. Label-free quantification - Wikipedia

    en.wikipedia.org/wiki/Label-free_quantification

    Label-free quantification is a method in mass spectrometry that aims to determine the relative amount of proteins in two or more biological samples. Unlike other methods for protein quantification, label-free quantification does not use a stable isotope containing compound to chemically bind to and thus label the protein. [1] [2]

  5. Protein methods - Wikipedia

    en.wikipedia.org/wiki/Protein_methods

    Protein methods are the techniques used to study proteins.There are experimental methods for studying proteins (e.g., for detecting proteins, for isolating and purifying proteins, and for characterizing the structure and function of proteins, [1] often requiring that the protein first be purified).

  6. Quantitative proteomics - Wikipedia

    en.wikipedia.org/wiki/Quantitative_proteomics

    The concentration of a certain protein in a sample may be determined using spectrophotometric procedures. [5] The concentration of a protein can be determined by measuring the OD at 280 nm on a spectrophotometer, which can be used with a standard curve assay to quantify the presence of tryptophan, tyrosine, and phenylalanine. [6]

  7. Lowry protein assay - Wikipedia

    en.wikipedia.org/wiki/Lowry_protein_assay

    The Lowry protein assay is a biochemical assay for determining the total level of protein in a solution. The total protein concentration is exhibited by a color change of the sample solution in proportion to protein concentration, which can then be measured using colorimetric techniques .

  8. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    An active site titration process can be done for the elimination of errors arising from differences in cultivation batches and/or misfolded enzyme and similar issues. This is a measure of the amount of active enzyme, calculated by e.g. titrating the amount of active sites present by employing an irreversible inhibitor.

  9. Dumas method - Wikipedia

    en.wikipedia.org/wiki/Dumas_method

    The Dumas technique has been automated and instrumentalized, so that it is capable of rapidly measuring the crude protein concentration of food samples. This automatic Dumas technique has replaced the Kjeldahl method as the standard method of analysis for nutritional labelling of protein content of foods (except in high fat content foods where ...

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