On the molecular basis of pyruvate kinase deficiency
| Autor: | K.G. Blume, H. Arnold, G.W. Löhr, G. Scholz |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Pyruvate decarboxylation
Heterozygote Erythrocytes Hot Temperature Pyruvate dehydrogenase kinase Pyruvate Kinase PKM2 Biology Pyruvate dehydrogenase phosphatase Anemia Hemolytic Congenital Phosphoenolpyruvate Drug Stability Hexokinase medicine Humans Fructosephosphates General Medicine Pyruvate dehydrogenase complex medicine.disease Glutathione Molecular biology Pyruvate carboxylase Adenosine Diphosphate Kinetics Glutathione Reductase Biochemistry Flavin-Adenine Dinucleotide Female Hexosediphosphates Oxidation-Reduction Pyruvate kinase Pyruvate kinase deficiency |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Enzymology. 370:601-604 |
| ISSN: | 0005-2744 |
| Popis: | Oxidized glutathione was found to be in the normal range in pyruvate kinase (ATP: pyruvate 2-O- phosphotransferase , EC 2.7.1.40) deficient erythrocytes and in erythrocytes from obligate heterozygotes with this inborn error of metabolism. Physiological concentrations of oxidized glutathione failed to affect the kinetics and stability of pyruvate kinase. From the data reported in this paper it seems to be unlikely that pyruvate kinase deficiency is the consequence of an increased oxidized glutathione concentration in the red blood cell. |
| Databáze: | OpenAIRE |
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