[Oxidation in glutathione and NADP system and GSSG liberation in extracellular spaces using hydroperoxide in the hemoglobin-free perfused rat liver]. 1972

H Sies, and C Gerstenecker, and H Menzel, and L Flohé

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D009249 NADP Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed) Coenzyme II,Nicotinamide-Adenine Dinucleotide Phosphate,Triphosphopyridine Nucleotide,NADPH,Dinucleotide Phosphate, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide Phosphate,Nucleotide, Triphosphopyridine,Phosphate, Nicotinamide-Adenine Dinucleotide
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010477 Perfusion Treatment process involving the injection of fluid into an organ or tissue. Perfusions
D010544 Peroxidases Ovoperoxidase
D005110 Extracellular Space Interstitial space between cells, occupied by INTERSTITIAL FLUID as well as amorphous and fibrous substances. For organisms with a CELL WALL, the extracellular space includes everything outside of the CELL MEMBRANE including the PERIPLASM and the cell wall. Intercellular Space,Extracellular Spaces,Intercellular Spaces,Space, Extracellular,Space, Intercellular,Spaces, Extracellular,Spaces, Intercellular
D005978 Glutathione A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides. Reduced Glutathione,gamma-L-Glu-L-Cys-Gly,gamma-L-Glutamyl-L-Cysteinylglycine,Glutathione, Reduced,gamma L Glu L Cys Gly,gamma L Glutamyl L Cysteinylglycine
D005980 Glutathione Reductase 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. Glutathione-Disulfide Reductase,Reductase, Glutathione,Reductase, Glutathione-Disulfide
D006454 Hemoglobins The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D006861 Hydrogen Peroxide A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials. Hydrogen Peroxide (H2O2),Hydroperoxide,Oxydol,Perhydrol,Superoxol,Peroxide, Hydrogen

Related Publications

H Sies, and C Gerstenecker, and H Menzel, and L Flohé
August 1973, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
H Sies, and C Gerstenecker, and H Menzel, and L Flohé
August 1971, Chemico-biological interactions,
H Sies, and C Gerstenecker, and H Menzel, and L Flohé
March 1989, The American journal of physiology,
H Sies, and C Gerstenecker, and H Menzel, and L Flohé
March 1981, The Journal of pharmacology and experimental therapeutics,
H Sies, and C Gerstenecker, and H Menzel, and L Flohé
September 1984, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
H Sies, and C Gerstenecker, and H Menzel, and L Flohé
July 1990, Journal of biochemistry,
H Sies, and C Gerstenecker, and H Menzel, and L Flohé
January 1978, The Journal of biological chemistry,
Copied contents to your clipboard!