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  2. 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%.

  3. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  4. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    During enzyme catalytic reaction, the substrate and active site are brought together in a close proximity. This approach has various purposes. Firstly, when substrates bind within the active site the effective concentration of it significantly increases than in solution. This means the number of substrate molecules involved in the reaction is ...

  5. Lysis buffer - Wikipedia

    en.wikipedia.org/wiki/Lysis_buffer

    The specific combination and concentrations of detergents, salts, and enzymes in lysing buffers can vary depending on the target enzyme, cell type, and experimental requirements, optimization of these components is crucial to achieve efficient cell lysis while preserving the stability and activity of the desired enzyme during the purification ...

  6. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    The primary difference between competitive and non-competitive is that competitive inhibition affects the substrate's ability to bind by binding an inhibitor in place of a substrate, which lowers the affinity of the enzyme for the substrate. In non-competitive inhibition, the inhibitor binds to an allosteric site and prevents the enzyme ...

  7. Gel electrophoresis of proteins - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis_of...

    Proteins separated by SDS-PAGE, Coomassie brilliant blue staining. Protein electrophoresis is a method for analysing the proteins in a fluid or an extract. The electrophoresis may be performed with a small volume of sample in a number of alternative ways with or without a supporting medium, namely agarose or polyacrylamide.

  8. Polyphenol oxidase - Wikipedia

    en.wikipedia.org/wiki/Polyphenol_oxidase

    In plants, PPO is a plastidic enzyme with unclear synthesis and function. In functional chloroplasts, it may be involved in oxygen chemistry like mediation of pseudocyclic photophosphorylation. [15] Enzyme nomenclature differentiates between monophenol oxidase enzymes (tyrosinases) and o-diphenol:oxygen oxidoreductase enzymes (catechol oxidases).

  9. Zymogen - Wikipedia

    en.wikipedia.org/wiki/Zymogen

    In biochemistry, a zymogen (/ ˈ z aɪ m ə dʒ ən,-m oʊ-/ [1] [2]), also called a proenzyme (/ ˌ p r oʊ ˈ ɛ n z aɪ m / [3] [4]), is an inactive precursor of an enzyme.A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme.