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  2. Iodine–starch test - Wikipedia

    en.wikipedia.org/wiki/Iodine–starch_test

    The cut surface of an apple stained with iodine, indicating a starch level of 4–5. The iodine–starch test is a chemical reaction that is used to test for the presence of starch or for iodine. The combination of starch and iodine is intensely blue-black. [1] [2] The interaction between starch and the triiodide anion (I − 3) is the basis ...

  3. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    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.

  4. Minor test - Wikipedia

    en.wikipedia.org/wiki/Minor_test

    The Minor test (also known as Minor's test, the starch–iodine test, and the iodine–starch test), described by Victor Minor in 1928, [1] is a qualitative medical test that is used to evaluate sudomotor function (perspiration or sweating).

  5. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    Partially hydrolysed potato starch makes for another non-toxic medium for protein electrophoresis. The gels are slightly more opaque than acrylamide or agarose. Non-denatured proteins can be separated according to charge and size. They are visualised using Napthal Black or Amido Black staining. Typical starch gel concentrations are 5% to 10%.

  6. Methods to investigate protein–protein interactions - Wikipedia

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

    The protein of interest is isolated with a specific antibody. Interaction partners which stick to this protein are subsequently identified by Western blotting. [2] Interactions detected by this approach are considered to be real. However, this method can only verify interactions between suspected interaction partners.

  7. Protein methods - Wikipedia

    en.wikipedia.org/wiki/Protein_methods

    Protein purification is a critical process in molecular biology and biochemistry, aimed at isolating a specific protein from a complex mixture, such as cell lysates or tissue extracts. [9] The goal is to obtain the protein in a pure form that retains its biological activity for further study, including functional assays, structural analysis, or ...

  8. Category:Laboratory techniques - Wikipedia

    en.wikipedia.org/wiki/Category:Laboratory_techniques

    Immunohistochemistry test; Immunomagnetic separation; Immunoperoxidase; Immunosequencing; Impalefection; In situ hybridization; In vitro; Indirect immunoperoxidase assay; Induced cell cycle arrest; Inert salt; Intravital microscopy; Inverse polymerase chain reaction; Iodine–starch test; Ion-mobility spectrometry–mass spectrometry; Ion ...

  9. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Specific activity is equal to the rate of reaction multiplied by the volume of reaction divided by the mass of total protein. The SI unit is katal/kg, but a more practical unit is μmol/(mg*min). Specific activity is a measure of enzyme processivity (the capability of enzyme to be processed), at a specific (usually saturating) substrate ...