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  2. Urease - Wikipedia

    en.wikipedia.org/wiki/Urease

    In vitro activation also has been achieved with manganese and cobalt in place of nickel. [8] Lead salts are inhibiting. The molecular weight is either 480 kDa or 545 kDa for jack-bean urease (calculated mass from the amino acid sequence). 840 amino acids per molecule, of which 90 are cysteine residues. [9]

  3. Phage display - Wikipedia

    en.wikipedia.org/wiki/Phage_display

    Phage display is also a widely used method for in vitro protein evolution (also called protein engineering). As such, phage display is a useful tool in drug discovery. It is used for finding new ligands (enzyme inhibitors, receptor agonists and antagonists) to target proteins.

  4. Cell-free protein synthesis - Wikipedia

    en.wikipedia.org/wiki/Cell-free_protein_synthesis

    Cell-free protein synthesis, also known as in vitro protein synthesis or CFPS, is the production of protein using biological machinery in a cell-free system, that is, without the use of living cells. The in vitro protein synthesis environment is not constrained by a cell wall or homeostasis conditions necessary to maintain cell viability. [ 1 ]

  5. Protein therapeutics - Wikipedia

    en.wikipedia.org/wiki/Protein_therapeutics

    Protein therapeutics are proteins used as experimental or approved therapies for disease states. They include "monoclonal antibodies (mAbs), peptide hormones, growth factors, plasma proteins, enzymes, and hemolytic factors" [1] While proteins can be more specific and flexible in their mechanism of action compared to small-molecule drugs, duration of action and drug delivery can be a challenge.

  6. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    In 1926, James B. Sumner showed that the enzyme urease was a pure protein and crystallized it; he did likewise for the enzyme catalase in 1937. The conclusion that pure proteins can be enzymes was definitively demonstrated by John Howard Northrop and Wendell Meredith Stanley , who worked on the digestive enzymes pepsin (1930), trypsin and ...

  7. Cytosine deaminase - Wikipedia

    en.wikipedia.org/wiki/Cytosine_deaminase

    In enzymology, a cytosine deaminase (EC 3.5.4.1) is an enzyme that catalyzes the chemical reaction. cytosine + H 2 O uracil + NH 3. Thus, the two substrates of this enzyme are cytosine [1] and H 2 O, whereas its two products are uracil and NH 3.

  8. Diagnostic microbiology - Wikipedia

    en.wikipedia.org/wiki/Diagnostic_Microbiology

    The urease agar slant is used to measure an organism’s ability to produce urease, an enzyme capable to digesting urea in carbon dioxide and ammonia through hydrolysis. Because ammonia is alkaline, the media contains phenol red, an indicator that changes from orange to pink when a pH increases above 8.1.

  9. Enzyme replacement therapy - Wikipedia

    en.wikipedia.org/wiki/Enzyme_replacement_therapy

    In gene therapy, a gene encoding for a certain protein is inserted into a vector. [11] The vector containing the therapeutic gene is then injected into the patient. [11] Once inside the body the vector introduces the therapeutic gene into host cells, and the protein encoded by the newly inserted gene is then produced by the body's own cells. [11]