Robin D. Powell, M.D.; Richard L. DeGowin, M.D.
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Pyruvate kinase catalyzes a key, adenosine triphosphate-generating step of anaerobic glycolysis. This pathway constitutes the main source of energy in mature erythrocytes of human beings. We have studied the activity of pyruvate kinase in hemolysates of erythrocytes from normal and from glucose-6-phosphate dehydrogenase (G6PD)-deficient American Negro men. G6PD-deficient erythrocytes are susceptible to drug-induced hemolysis. The life span of G6PD-deficient erythrocytes in vivo is shorter than normal, even in the absence of hemolytic drugs, and older G6PD-deficient erythrocytes are more susceptible to hemolysis than are younger cells.
The mean activity of pyruvate kinase in hemolysates of erythrocytes from 12 G6PD-deficient men
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Powell RD, DeGowin RL. Studies on the Activity of Pyruvate Kinase in Hemolysates of Normal and Glucose-6-Phosphate Dehydrogenase-deficient Erythrocytes.. Ann Intern Med. 1965;62:1086. doi: 10.7326/0003-4819-62-5-1086_1
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Published: Ann Intern Med. 1965;62(5):1086.
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Print ISSN: 0003-4819 | Online ISSN: 1539-3704
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