NADPH-flavin reductase in human erythrocytes and the reduction of methemoglobin through flavin by the enzyme. 1977

T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama

UI MeSH Term Description Entries
D008706 Methemoglobin Ferrihemoglobin
D008751 Methylene Blue A compound consisting of dark green crystals or crystalline powder, having a bronze-like luster. Solutions in water or alcohol have a deep blue color. Methylene blue is used as a bacteriologic stain and as an indicator. It inhibits GUANYLATE CYCLASE, and has been used to treat cyanide poisoning and to lower levels of METHEMOGLOBIN. Methylthionine Chloride,Swiss Blue,Basic Blue 9,Chromosmon,Methylene Blue N,Methylthioninium Chloride,Urolene Blue,Blue 9, Basic,Blue N, Methylene,Blue, Methylene,Blue, Swiss,Blue, Urolene
D009247 NADH, NADPH Oxidoreductases A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6. Oxidoreductases, NADH, NADPH,NADPH Oxidoreductases NADH,Oxidoreductases NADH, NADPH
D009252 NADPH Dehydrogenase A flavoprotein that reversibly oxidizes NADPH to NADP and a reduced acceptor. EC 1.6.99.1. NADP Dehydrogenase,NADP Diaphorase,NADPH Diaphorase,Old Yellow Enzyme,TPN Diaphorase,Dehydrogenase, NADP,Dehydrogenase, NADPH,Diaphorase, NADP,Diaphorase, NADPH,Diaphorase, TPN,Enzyme, Old Yellow
D004912 Erythrocytes Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN. Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D005182 Flavin-Adenine Dinucleotide A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972) FAD,Flavitan,Dinucleotide, Flavin-Adenine,Flavin Adenine Dinucleotide
D005415 Flavins Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.
D005486 Flavin Mononucleotide A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues. FMN,Flavin Mononucleotide Disodium Salt,Flavin Mononucleotide Monosodium Salt,Flavin Mononucleotide Monosodium Salt, Dihydrate,Flavin Mononucleotide Sodium Salt,Riboflavin 5'-Monophosphate,Riboflavin 5'-Phosphate,Riboflavin Mononucleotide,Sodium Riboflavin Phosphate,5'-Monophosphate, Riboflavin,5'-Phosphate, Riboflavin,Mononucleotide, Flavin,Mononucleotide, Riboflavin,Phosphate, Sodium Riboflavin,Riboflavin 5' Monophosphate,Riboflavin 5' Phosphate,Riboflavin Phosphate, Sodium
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012256 Riboflavin Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE. Vitamin B 2,Vitamin G,Vitamin B2

Related Publications

T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
June 1980, Journal of biochemistry,
T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
September 1981, Archives of biochemistry and biophysics,
T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
August 1987, Nihon Ika Daigaku zasshi,
T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
January 1981, Progress in clinical and biological research,
T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
May 1980, The Journal of biological chemistry,
T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
July 1987, Biochemistry international,
T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
April 1979, The Biochemical journal,
T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
December 2012, Fish physiology and biochemistry,
T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
October 1971, The Journal of biological chemistry,
T Yubisui, and T Matsuki, and K Tanishima, and M Takeshita, and Y Yoneyama
December 1987, Nihon Ika Daigaku zasshi,
Copied contents to your clipboard!