enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Type I topoisomerase - Wikipedia

    en.wikipedia.org/wiki/Type_I_topoisomerase

    The enzyme uses the hydrolysis of ATP to introduce positive supercoils and overwinds DNA, a feature attractive in hyperthermophiles, in which reverse gyrase is known to exist. Rodriguez and Stock have done further work to identify a "latch" that is involved in communicating the hydrolysis of ATP to the introduction of positive supercoils.

  3. Affinity chromatography - Wikipedia

    en.wikipedia.org/wiki/Affinity_chromatography

    Weak affinity chromatography [29] (WAC) is an affinity chromatography technique for affinity screening in drug development. [ 30 ] [ 31 ] WAC is an affinity-based liquid chromatographic technique that separates chemical compounds based on their different weak affinities to an immobilized target.

  4. Affinity label - Wikipedia

    en.wikipedia.org/wiki/Affinity_label

    The hallmark of an affinity label is the use of a targeting moiety to specifically and reversibly deliver a weakly reactive group to the enzyme that irreversibly binds to an amino acid residue. The targeting portion of the label often resembles the enzyme's natural substrate so that a similar mode of noncovalent binding is used prior to the ...

  5. Cooperative binding - Wikipedia

    en.wikipedia.org/wiki/Cooperative_binding

    The first description of cooperative binding to a multi-site protein was developed by A.V. Hill. [4] Drawing on observations of oxygen binding to hemoglobin and the idea that cooperativity arose from the aggregation of hemoglobin molecules, each one binding one oxygen molecule, Hill suggested a phenomenological equation that has since been named after him:

  6. Mixed inhibition - Wikipedia

    en.wikipedia.org/wiki/Mixed_inhibition

    a possible mechanism of non-competitive inhibition, a kind of mixed inhibition.. Mixed inhibition is a type of enzyme inhibition in which the inhibitor may bind to the enzyme whether or not the enzyme has already bound the substrate but has a greater affinity for one state or the other. [1]

  7. Industrial enzymes - Wikipedia

    en.wikipedia.org/wiki/Industrial_enzymes

    Immobilization using affinity relies on the specificity of an enzyme to couple an affinity ligand to an enzyme to form a covalently bound enzyme-ligand complex. The complex is introduced into a support matrix for which the ligand has high binding affinity, and the enzyme is immobilized through ligand-support interactions. [3]

  8. Affinity electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Affinity_electrophoresis

    The methods have been used for estimation of binding constants, as for instance in lectin affinity electrophoresis or characterization of molecules with specific features like glycan content or ligand binding. [1] For enzymes and other ligand-binding proteins, one-dimensional electrophoresis similar to counter electrophoresis or to "rocket ...

  9. Arginase - Wikipedia

    en.wikipedia.org/wiki/Arginase

    The enzymes in the kidney will then catalyze ureagenesis, compensating somewhat for a decrease in arginase I activity in the liver. Due to this alternate method of removing excess arginine and ammonia from the bloodstream, subjects with arginase deficiency tend to have longer lifespans than those who have other urea cycle defects.