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  2. Glutathione S-transferase A1 - Wikipedia

    en.wikipedia.org/wiki/Glutathione_S-transferase_A1

    These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of some drugs. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta.

  3. Glutathione synthetase deficiency - Wikipedia

    en.wikipedia.org/wiki/Glutathione_synthetase...

    Glutathione synthetase deficiency has an autosomal recessive pattern of inheritance. Mutations in the GSS gene cause glutathione synthetase deficiency. This gene provides instructions for making the enzyme glutathione synthetase. This enzyme is involved in a process called the gamma-glutamyl cycle, which takes place in most of the body's cells ...

  4. GSTA2 - Wikipedia

    en.wikipedia.org/wiki/GSTA2

    The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver. In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity thereby protecting the cells from reactive oxygen ...

  5. Glutathione synthetase - Wikipedia

    en.wikipedia.org/wiki/Glutathione_synthetase

    Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione. [2] Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants. [3]

  6. What You Need to Know About Glutathione, a Powerful ... - AOL

    www.aol.com/know-glutathione-powerful...

    Plus, glutathione side effects and dosages. Here, find the health benefits of glutathione, an antioxidant that helps make proteins in the body. Plus, glutathione side effects and dosages.

  7. Glutathione S-transferase - Wikipedia

    en.wikipedia.org/wiki/Glutathione_S-transferase

    The glutathione binding site, or "G-site", is located in the thioredoxin-like domain of both cytosolic and mitochondrial GSTs. The region containing the greatest amount of variability between the assorted classes is that of helix α2, where one of three different amino acid residues interacts with the glycine residue of

  8. GSTT2 - Wikipedia

    en.wikipedia.org/wiki/GSTT2

    Glutathione S-transferase theta-2 is an enzyme that in humans is encoded by the GSTT2 gene. [ 5 ] [ 6 ] [ 7 ] Glutathione S-transferase (GSTs) theta 2 (GSTT2) is a member of a superfamily of proteins that catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds.

  9. Polyol pathway - Wikipedia

    en.wikipedia.org/wiki/Polyol_pathway

    The amount of sorbitol that accumulates, however, may not be sufficient to cause osmotic influx of water. NADPH acts to promote nitric oxide production and glutathione reduction, and its deficiency will cause glutathione deficiency. A glutathione deficiency, congenital or acquired, can lead to hemolysis caused by oxidative stress.

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