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  2. Glutathione - Wikipedia

    en.wikipedia.org/wiki/Glutathione

    Glutathione (GSH, / ˌɡluːtəˈθaɪoʊn /) is an organic compound with the chemical formula HOCOCH (NH2)CH2CH2CONHCH (CH2SH)CONHCH2COOH. It is an antioxidant in plants, animals, fungi, and some bacteria and archaea. Glutathione is capable of preventing damage to important cellular components caused by sources such as reactive oxygen species ...

  3. 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.

  4. Glutathione reductase - Wikipedia

    en.wikipedia.org/wiki/Glutathione_reductase

    Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene.Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide to the sulfhydryl form glutathione (), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell.

  5. Glutathione May Have Major Benefits For Your Skin ... - AOL

    www.aol.com/lifestyle/glutathione-may-major...

    Increasing levels of glutathione in the body may help slow down the rate of progressive neural tissue damage in these conditions, a 2014 study in the Journal of Alzheimer's Disease found. But Dr ...

  6. Glutathione peroxidase 4 - Wikipedia

    en.wikipedia.org/wiki/Glutathione_peroxidase_4

    The antioxidant enzyme glutathione peroxidase 4 (GPX4) belongs to the family of glutathione peroxidases, which consists of 8 known mammalian isoenzymes (GPX1–8).GPX4 catalyzes the reduction of hydrogen peroxide, organic hydroperoxides, and lipid peroxides at the expense of reduced glutathione and functions in the protection of cells against oxidative stress.

  7. Glutaredoxin - Wikipedia

    en.wikipedia.org/wiki/Glutaredoxin

    PDBsum. structure summary. Glutaredoxins[1][2][3] (also known as Thioltransferase) are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. In humans this oxidation repair enzyme is also known to participate in many cellular functions, including redox signaling and regulation of glucose ...

  8. Glutathione S-transferase A1 - Wikipedia

    en.wikipedia.org/wiki/Glutathione_S-transferase_A1

    Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene. [5] Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and ...

  9. Glutamine - Wikipedia

    en.wikipedia.org/wiki/Glutamine

    Glutamine (data page) Glutamine (symbol Gln or Q) [4] is an α-amino acid that is used in the biosynthesis of proteins. Its side chain is similar to that of glutamic acid, except the carboxylic acid group is replaced by an amide. It is classified as a charge-neutral, polar amino acid.