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  2. 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]

  3. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amino group is removed from the amino acid and converted to ammonia.

  4. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    At high temperatures, these interactions cannot form, and a functional protein is denatured. [25] However, it relies on two factors; the type of protein used and the amount of heat applied. The amount of heat applied determines whether this change in protein is permanent or if it can be transformed back to its original form. [26]

  5. Catabolism - Wikipedia

    en.wikipedia.org/wiki/Catabolism

    Catabolism breaks down large molecules (such as polysaccharides, lipids, nucleic acids, and proteins) into smaller units (such as monosaccharides, fatty acids, nucleotides, and amino acids, respectively). Catabolism is the breaking-down aspect of metabolism, whereas anabolism is the building-up aspect.

  6. Proteinase K - Wikipedia

    en.wikipedia.org/wiki/Proteinase_K

    The enzyme's activity towards native proteins is stimulated by denaturants such as SDS. In contrast, when measured using peptide substrates, denaturants inhibit the enzyme. The reason for this result is that the denaturing agents unfold the protein substrates and make them more accessible to the protease. [8]

  7. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    The products usually are either alanine, aspartate or glutamate, since their corresponding alpha-keto acids are produced through metabolism of fuels. Being a major degradative aminoacid pathway, lysine , proline and threonine are the only three amino acids that do not always undergo transamination and rather use respective dehydrogenase.

  8. Purine metabolism - Wikipedia

    en.wikipedia.org/wiki/Purine_metabolism

    Methotrexate also indirectly inhibits purine synthesis by blocking the metabolism of folic acid (it is an inhibitor of the dihydrofolate reductase). Allopurinol is a drug that inhibits the enzyme xanthine oxidoreductase and, thus, lowers the level of uric acid in the body. This may be useful in the treatment of gout, which is a disease caused ...

  9. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein.