Deficient Activity of DPNH-dependent Methemoglobin Diaphorase in Cord Blood Erythrocytes
نویسندگان
چکیده
منابع مشابه
Deficient activity of DPNH-dependent methemoglobin diaphorase in cord blood erythrocytes.
Y OUNG INFANTS are unusually susceptible to the development of methemoglobinemia upon exposure to certain medications and toxic agents. Ingestion of well water containing large quantities of nitrate will cause methemoglobinemia in small babies while older members of the family remain unaffected.14 Bismuth subnitrate, benzocaine, resorcin or aniline dye, taken by mouth or absorbed rectally or pe...
متن کاملNAD(P) glycohydrolase deficiency in human erythrocytes and alteration of cytosol NADH-methemoglobin diaphorase by membrane NAD-glycohydrolase activity.
Erythrocytic NADH methemoglobin diaphorase acquires NADH-dichlorophenolindophenol diaphorase activity when enzyme-associated NAD is removed. This transformation is reversible and can be mediated by membrane NAD glycohydrolase (EC 3.2.2.5) in hemolysates as well as in intact cells exposed to hydrogen peroxide. It is abolished either in NADH methemoglobin diaphorase deficiency or in NAD(P) glycoh...
متن کامل[Regulation of methemoglobin reduction in human erythrocytes].
The regulation of methemoglobin reduction in human erythrocytes was studied in vitro in association with glycolytic reactions, by using hemolysates prepared from the nitrate-treated eryth rocytes. The results obtained are as follows; 1) The addition of cytochrome b5 to the reaction mixture containing fructose 1,6-diphosphate as the substrate for glycolysis caused a marked increase in...
متن کاملProtective Effect of Quercetin on Oxidative Stress in Glucose-6-Phosphate Dehydrogenase-Deficient Erythrocytes in Vitro
Glucose-6-phosphate dehydrogenase (G6PD) deficient subjects are vulnerable to oxidative stress. Quercetin, a flavonoids, has been employed as a potent oxygen-free radical scavenger in order to assess the protective effects of quercetin against H2O2-induced oxidative damage in G6PD-deficient and normal human erythrocytes. Erythrocytes of G6PD-deficient (n = 10) and normal (n = 10) subjects were ...
متن کاملCharacterization of NADPH-dependent methemoglobin reductase as a heme-binding protein present in erythrocytes and liver.
An NADPH-dependent reductase, first shown in the 1930s to catalyze the methylene blue-dependent reduction of methemoglobin in erythrocytes, has now been characterized as a high-affinity heme-binding protein and has been detected in liver. Highly purified bovine erythrocyte reductase binds protohemin to form a 1:1 complex with a Kd of 7 nM. Binding of protohemin completely inhibits reductase act...
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ژورنال
عنوان ژورنال: Blood
سال: 1963
ISSN: 0006-4971,1528-0020
DOI: 10.1182/blood.v21.1.51.51