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  • aldehyde reductase
    ¾Ëµ¥È÷µåȯ¿øÈ¿¼Ò
  • reductase
    ȯ¿øÈ¿¼Ò
  • glutathione
    ±Û·çŸƼ¿Â
  • glutathione peroxidase
    ±Û·çŸƼ¿Â°ú»êÈ­È¿¼Ò
  • glutathione synthetase
    ±Û·çŸƼ¿ÂÇÕ¼ºÈ¿¼Ò
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  • glutathione
    ±Û·çŸƼ¿Â
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  • reductase
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  • glutathione
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  • glutathione peroxidase
    ±Û·çŸƼ¿Â°ú»êÈ­È¿¼Ò
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  • glutathione reductase
    ±Û·çŸƼ¿Â ¸®´ÚŸÁ¦<ȯ¿øÈ¿¼Ò>.
  • glutathione reductase
    ±Û·çŸƼ¿Â¸®´ÚŸÁ¦<--ȯ¿øÈ¿¼Ò>
  • glutathione reductase deficiency
    ±Û·çŸƼ¿Â ȯ¿øÈ¿¼Ò °áÇÌÁõ.
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  • reductase, 5-alpha-reductase inhibitor
    5a-ȯ¿øÈ¿¼Ò¾ïÁ¦Á¦(¡­ü½êªý£áÈåäð¤ð¥),5a-¸®´öÅ×À̽º¾ïÁ¦Á¦(¡­åäð¤ð¥)
  • glutathione
    ±Û·çŸƼ¿Â.
  • glutathione
    ±Û·çŸƼ¿Â
  • glutathione peroxidase
    ±Û·çŸƼ¿Â Æä¸£¿Á½Ã´ÙÁ¦<°ú»êÈ­È¿¼Ò>.
  • glutathione peroxidase
    ±Û·çŸƼ¿ÂÆä¸£¿Á½Ã´ÙÁ¦(°ú»êÈ­ È¿¼Ò)
  • glutathione peroxidase
    ±Û·çŸƼ¿ÂÆä¸£¿Á½Ã´ÙÁ¦<--°ú»êÈ­ È¿¼Ò>
  • NADH-cytochrome b5 reductase
    NADH-½ÃÅäÅ©·Òb5¸®´öŸ¾ÆÁ¦
  • NADH-methemoglobin reductase
    NADH-¸ÞÆ®Çì¸ð±Û·Îºó ȯ¿øÈ¿¼Ò
  • NADPH-dependent methemoglobin reductase
    NADH-ÀÇÁ¸¸ÞÆ®Çì¸ð±Û·Îºó ¸®´öŸ¾ÆÁ¦
  • glyoxylate reductase
    ±Û¸®¿Á½Ç»êȯ¿øÈ¿¼Ò.
  • reductase
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  • reductase
    ȯ¿øÈ¿¼Ò
  • reductase test
    ȯ¿øÈ¿¼Ò½ÃÇè.
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  • glutathione reductase
    ±Û·çŸƼ¿Â¸®´ÚŸÁ¦<--ȯ¿øÈ¿¼Ò>
  • glutathione reductase
    ±Û·çŸƼ¿Â ¸®´ÚŸÁ¦<ȯ¿øÈ¿¼Ò>.
  • glutathione reductase deficiency
    ±Û·çŸƼ¿Â ȯ¿øÈ¿¼Ò °áÇÌÁõ.
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  • reductase, 5-alpha-reductase inhibitor
    5a-ȯ¿øÈ¿¼Ò¾ïÁ¦Á¦(¡­ü½êªý£áÈåäð¤ð¥),5a-¸®´öÅ×À̽º¾ïÁ¦Á¦(¡­åäð¤ð¥)
  • glutathione
    ±Û·çŸƼ¿Â
  • glutathione
    ±Û·çŸƼ¿Â.
  • glutathione peroxidase
    ±Û·çŸƼ¿ÂÆä¸£¿Á½Ã´ÙÁ¦<--°ú»êÈ­ È¿¼Ò>
  • glutathione peroxidase
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  • glutathione peroxidase
    ±Û·çŸƼ¿ÂÆä¸£¿Á½Ã´ÙÁ¦(°ú»êÈ­ È¿¼Ò)
  • glutathione synthetase
    ±Û·çŸƼ¿ÂÇÕ¼ºÈ¿¼Ò
  • cystine reductase
    ½Ã½ºÆ¾È¯¿øÈ¿¼Ò(¡­ü½êª ý£áÈ).
  • cytochrome b5 reductase deficiency
    ½ÃÅäÅ©·Ò b5 ȯ¿øÈ¿¼Ò °áÇÌ
  • cytochrome reductase
    ½ÃÅäÅ©·Ò ·¹´ÚŸÁ¦<ȯ¿øÈ¿¼Ò(ü½êªý£áÈ)>.
  • dihydropteridine reductase
    Dihydropteridine reductase
  • glyoxylate reductase
    ±Û¸®¿Á½Ç»êȯ¿øÈ¿¼Ò.
  • glyoxylic acid reductase deficency
  • reductase
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  • reductase
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  • glutathione
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  • glutathione-S-transferase
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  • coenzyme Q-cytochrome c reductase complex
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  • dihydrofolate reductase
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  • folic acid reductase
    Æú»ê(ß«) ¸®´ÚÅ×À̽º
  • nitrate reductase
    Áú»ê(òòß«) ¸®´ÚÅ×À̽º
  • nitrite reductase
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  • reductase
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  • ribonucleotide reductase
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  • succinate-coenzyme Q reductase
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  • thioredoxin reductase
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E-GR erythrocyte glutathione reductase
EGRAC erythrocyte glutathione reductase activity coefficient
GR gamma-rays; gastric resection; general research; generalized rash; glucocorticoid receptor; glutathi...
GSR galvanic skin response; generalized Shwartzman reaction; glutathione reductase
GSSG-R glutathione reductase
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GR Glutathione reductase
E-GR erythrocyte glutathione reductase
EGR-AC erythrocyte glutathione reductase activity coefficient
GRD glutathione reductase
HMG-CoA reductase 3-Hydroxy-3-methylglutaryl CoA reductase
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  • acetaldehyde reductase
    ¾Æ¼¼Æ® ¾Ëµ¥ÇÏÀ̵å ȯ¿ø È¿¼Ò
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glutathione reductase <enzyme> An FAD containing enzyme, a dimer of 50 kD subunits.
It catalyses the NADP dependent reduction of glutathione disulphide (GSSG) to glutathione (GSH). This is an essential reaction that maintains a GSH:GSSG ratio in the cytoplasm of _500:1.
(18 Nov 1997)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
protein disulfide reductase (glutathione) <enzyme> An enzyme that catalyses the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates.
Chemical name: Glutathione:protein-disulfide oxidoreductase
Registry number: EC 1.8.4.2
(12 Dec 1998)
reduced glutathione Glutathione acting as a hydrogen donor.
(05 Mar 2000)
glutathione <biochemistry> The tripeptide _ glutamylcysteinylglycine. It contains an unusual peptide linkage between the _ carboxyl group of the glutamate side chain and the amine group of cysteine.
The concentration of glutathione in animal cells is _5mM and its sulphydryl group is kept largely in the reduced state. This allows it to act as a sulphydryl buffer, reducing any disulphide bonds formed within cytoplasmic proteins to cysteines. Hence, few, if any, cytoplasmic proteins contain disulphide bonds.
Glutathione is also important as a cofactor for the enzyme glutathione peroxidase, in the uptake of amino acids and participates in leucotriene synthesis.
(18 Nov 1997)
glutathione disulfide <chemical> A glutathione derivative that forms when the sulfhydryl side chains of the cysteine residues of two glutathione molecules form a disulfide bond during the course of being oxidised with various oxides and peroxides in cells. Glutathione reductase, with the coupled oxidation of NADPH, reduces gssg to two moles of glutathione.
Chemical name: Bis(gamma-Glutamyl-L-cysteinylglycine) Disulfide
(12 Dec 1998)
glutathione oxidase <enzyme> Oxygen-dependent conversion of glutathione to glutathione disulfide
Registry number: EC 1.8.4.-
Synonym: renal thiol oxidase, renal sulfhydryl oxidase, intestinal thiol oxidase, kidney thiol oxidase
(26 Jun 1999)
glutathione peroxidase <enzyme> A detoxifying enzyme that eliminates hydrogen peroxide and organic peroxides.
Glutathione is an essential cofactor for the enzyme and its reaction involves the oxidation of glutathione (GSH) to glutathione disulphide (GSSG). The GSSG is then reduced to GSH by glutathione reductase. Glutathione peroxidase, (GPX), has a selenocysteine residue in its active site. Three forms of the enzyme exist: cy toplasmic GPX, plasma GPX and phospholipid hydroperoxide GPX.
(18 Nov 1997)
glutathione S-transferase A class of enzymes that catalyze the reaction of glutathione with an acceptor molecule (e.g., an arene oxide) to form an S-substituted glutathione; a key step in detoxification of many substances; start of the mercapturic acid pathway.
Synonym: ligandin.
(05 Mar 2000)
glutathione synthase <enzyme> One of the enzymes active in the gamma-glutamyl cycle. It catalyses the synthesis of glutathione from gamma-glutamylcysteine and glycine in the presence of ATP with the formation of ADP and orthophosphate.
Chemical name: gamma-L-Glutamyl-L-cysteine:glycine ligase (ADP-forming)
Registry number: EC 6.3.2.3
(12 Dec 1998)
glutathione synthetase <enzyme> An enzyme that catalyses the formation of glutathione, ADP, and orthophosphate from gamma-glutamylcysteine, ATP, and glycine; a deficiency will lead to metabolic acidosis and progressive brain dysfunction.
(05 Mar 2000)
glutathione synthetase deficiency An inborn error of metabolism associated with massive urinary excretion of 5-oxyproline, elevated levels of 5-oxyproline in the blood and cerebrospinal fluid, severe metabolic acidosis, tendency toward haemolysis, and defective central nervous systems function. Glutathione synthetase deficiency has been reported as a generalised condition or with a deficiency restricted to erythrocytes.
(05 Mar 2000)
glutathione transferase <enzyme> A transferase that catalyses the addition of aliphatic, aromatic, or heterocyclic radicals as well as epoxides and arene oxides to glutathione. Addition takes place at the sulfur atom. It also catalyses the reduction of polyol nitrate by glutathione to polyol and nitrite.
Chemical name: RX:glutathione R-transferase
Registry number: EC 2.5.1.18
(12 Dec 1998)
phospholipid-hydroperoxide glutathione peroxidase <enzyme> Selenoenzyme found in biological materials; different from glutathione peroxidase EC 1.11.1.9
Registry number: EC 1.11.1.-
Synonym: pH-gperoxidase
(26 Jun 1999)
S-(dinitrophenyl)glutathione ATPase <enzyme> Anionic conjugates of bilirubin and bile acids stimulate the hydrolysis of the above enzyme of human erythrocyte; also found in other tissue
Registry number: EC 3.6.1.-
Synonym: dnp-sg-atpase
(26 Jun 1999)
sulfobromophthalein-glutathione conjugase <enzyme> Similar to EC 2.5.1.18; non-microsomal enzyme involving transfer of the dye from plasma to hepatic parenchymal cells, cellular storage, enzymatic intracellular conjugation with reduced glutathione and rate limited excretion into the bile; activity of this enzyme is used to determine conjugating ability of the liver
Registry number: EC 2.5.1.-
Synonym: bromsulphthalein-glutathione conjugating enzyme
(26 Jun 1999)
oxidised glutathione <biochemistry> Glutathione acting in cells as a hydrogen acceptor; reduced by glutathione reductase.
(05 Mar 2000)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 1 ÆäÀÌÁö: 1
  • Glutathione Reductase - »õâ Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.
    Synonyms : Glutathione-Disulfide Reductase, Reductase, Glutathione, Reductase, Glutathione-Disulfide
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glutathione reductase An NADPH-dependent enzyme that reduces oxidized glutathione (GSSG) to GSH.
Ãâó: www.nature.com/focus/neurodegen/glossary/
glutathione reductase (NADPH) [EC 1.6.4.2] an enzyme of the oxidoreductase class that catalyzes the reduction of glutathione via oxidation of NADPH. It is a flavoprotein (FAD), occurring in erythrocytes, and is involved in many redox reactions. Deficiency of enzyme activity in erythrocytes usually results from nutritional or metabolic inadequacy of FAD and, except when severe, has not been linked to hemolysis. Diminished enzyme activity does decrease protection of cells from oxidative damage.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
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