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GR gamma-rays; gastric resection; general research; generalized rash; glucocorticoid receptor; glutathi...
GSD genetically significant dose; Gerstmann-Straussler disease; glutathione synthetase deficiency; glyco...
GSH glomerulus-stimulating hormone; golden Syrian hamster; reduced glutathione; L-alpha-glutamyl-L-cyste...
GSH-Px glutathione peroxidase
GSR galvanic skin response; generalized Shwartzman reaction; glutathione reductase
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GSTM1 Glutathione S-Transferase M1
GST-P Glutathione S-Transferase P
GT Glutathione S-transferase
GST Glutathione S-transferase activity
GST mu Glutathione S-transferase mu
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 2 ÆäÀÌÁö: 2
  • Glutathione Synthase - »õâ One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of glutathione from gamma-glutamylcysteine and glycine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.3.
    Synonyms : Synthase, Glutathione, Synthetase, Glutathione
  • Glutathione Transferase - »õâ A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
    Synonyms : Glutathione Organic Nitrate Ester Reductase, Glutathione S-Transferase, Glutathione S-Transferase 3, Glutathione S-Transferase A, Glutathione S-Transferase B, Glutathione S-Transferase C, Glutathione S-Transferase III, Glutathione S-Transferase P, Ligandin
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glutathione an antioxidant containing the amino acid cysteine which is needed for cellular production of energy and proper immune function. Glutathione has been reported to suppress HIV in vitro and may reduce HIV-related apoptosis (cell death).
Ãâó: www.aegis.com/ni/topics/glossary/g.asp
glutathione An abundant and essential antioxidant found within the cells that plays a huge role in the cell
Ãâó: www.nutros.com/nsr-05zzz.html
glutathione a tripeptide consisting of residues of glutamic acid, cysteine, and glycine, is known to act as a coenzyme in a few enzymatic reactions, but its importance may lie in its role as a nonspecific reducing agent within the cell. It is hypothesized that glutathione serves to maintain the biological activity of certain proteins by keeping selected cysteine sidechains in the reduced thiol form, thereby not allowing these residues to oxidize and cross-link with one another to form cystine residues. ...
Ãâó: www.bartleby.com/65/co/coenzyme.html
glutathione A tri-peptide, made from glutamic acid, cysteine, and glycine. It is the major anti-oxidant species in cells, and along with cysteine, it is critical for binding and detoxifying heavy metals. Levels of GSH are low in autism and the ratio of GSH to its oxidized form (GSSG) is low, indicating the presence of oxidation stress. GSH is also required for synthesis of methyl B12, so low levels can contribute to reduced methionine synthase activity.
Ãâó: www.thoughtfulhouse.org/0405-conf-glossary.htm
glutathione is a powerful anti-oxidant enzyme that requires the mineral selenium for its production.
Ãâó: www.optinutri.net/glossary.html
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