OXIDATIVE HEMOLYSIS AND ERYTHROCYTE METABOLISM IN HEREDITARY ACATALASIA.
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- Type
- article
- Published
- 1965-07-01
- Cited by
- 143
- References
- 38
- Access
- Open access
- OpenAlex
- https://openalex.org/W2077577363
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:12470857
Keywords
Hemolysis, Oxidative phosphorylation, Oxidative metabolism, Metabolism, Biochemistry
References
- Studies on the formation of Heinz bodies. II. The nature and significance of Heinz bodies.
- Effects of sulfhydryl inhibition on red blood cells. II. Studies in vivo.
- Properties of catalase. Catalysis of coupled oxidation of alcohols.
- Progressive oral gangrene probably due to lack of catalase in the blood (acatalasaemia); report of nine cases.
- Hematin Compounds and Bile Pigments; Their Constitution, Metabolism, and Function
- A PHOTOMETRIC ADAPTATION OF THE SOMOGYI METHOD FOR THE DETERMINATION OF GLUCOSE
- MICRODETERMINATION OF OXYHEMOGLOBIN, METHEMOGLOBIN, AND SULFHEMOGLOBIN IN A SINGLE SAMPLE OF BLOOD
- Thiol groups of biological importance.
- Effects of sulfhydryl inhibition on red blood cells. 3. Glutathione in the regulation of the hexose monophosphate pathway.
- Hemoglobin catabolism. II. The protection of hemoglobin from oxidative breakdown in the intact erythrocyte.
- Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown.
- Perborate as substrate in a new assay of catalase.
- A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase.
- Use of glucose oxidase, peroxidase, and O-dianisidine in determination of blood and urinary glucose.
- Primaquine sensitivity. Glucose-6-phosphate dehydrogenase deficiency: an inborn error of metabolism of medical and biological significance.
- Oxidation of Phenyl-Hydrazines in the Presence of Oxyhæmoglobin and the Origin of Heinz Bodies in Erythrocytes
- The formation of choleglobin and the role of catalase in the erythrocyte
- Effects of sulfhydryl inhibition on red blood cells. I. Mechanism of hemolysis.
- INCREASED CELL MEMBRANE PERMEABILITY IN THE PATHOGENESIS OF HEREDITARY SPHEROCYTOSIS.
- Progressive oral gangrene due to acatalasemia (colored motion picture) †
Cited by
- Increased membrane binding of erythrocyte catalase in hereditary spherocytosis and in metabolically stressed normal cells.
- Erythrocyte defense against hydrogen peroxide: preeminent importance of catalase.
- Studies of controlled reperfusion after ischemia. XXI. Reperfusate composition: superiority of blood cardioplegia over crystalloid cardioplegia in limiting reperfusion damage--importance of endogenous oxygen free radical scavengers in red blood cells.
- Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes.
- Relationships between iron-dextran and vitamin E in iron deficiency anemia in children.
- Radiation effects on biomembranes.
- NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes.
- OXIDAÇÃO DA HEMOGLOBINA COMO MODELO DE ESTUDO DO SISTEMA DE ÓXIDO-REDUÇÃO ERITROCITÁRIO: INTERAÇÃO ENTRE NITRITO DE SÓDIO, AZUL DE METILENO E CISTAMINA.
- Redox State Of Erythrocyte Peroxiredoxin 2 During Oxidative Stress And Its Effect On Membrane Binding
- Enhancement of erythrocyte superoxide dismutase activity: effects on cellular oxidant defense.
- Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes.
- Studies of the in vitro effects of oxidized glutathione and acetylphenylhydrazine on acid phosphatases of human red blood cells. An experimental model for the investigation of hemolytic drug action at the molecular level.
- Red cell metabolism in iron deficiency anemia. 3. The relationship between glutathione peroxidase, catalase, serum vitamin E, and susceptibility of iron-deficient red cells to oxidative hemolysis.
- Hydrogen peroxide toxicity and detoxification in the erythrocytes of newborn infants.
- Direct evidence for catalase as the predominant H2O2 -removing enzyme in human erythrocytes.
- Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasaemic Saccharomyces cerevisiae.
- Introduction to discussion of glucose-6-phosphate dehydrogenase deficiency.
- Dual labeling with a far red probe permits analysis of growth and oxidative stress in P. falciparum‐infected erythrocytes
- Decreased catalase activity is the underlying mechanism of oxidant susceptibility in glucose-6-phosphate dehydrogenase-deficient erythrocytes.
- Therapy with red blood cells decreases hyperoxic pulmonary injury.
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