| GSSG | oxidized glutathione |
|---|---|
| Adox | oxidized adenosine |
| Inox | inosine, oxidized |
| NAD+ | the oxidized form of NAD |
| NADP+ | oxidized form of nicotinamide adenine dinucleotide phosphate |
| OX | Oxidized |
|---|---|
| oATP | Oxidized ATP |
| DCVG | 1,2-dichlorovinyl glutathione |
| DNP-SG | 2,4-dinitrophenyl S-glutathione |
| alpha-GST | Alpha glutathione S-transferase |
| oxidized rhizosphere | Oxidized channels and soil surrounding living roots and rhizomes in plants. (09 Oct 1997) |
|---|---|
| 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 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) |
| 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) |
| 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) |
| 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) |
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|