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Response to Nance letter.
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A single amino Acid substitution (asparagine to aspartic Acid) between normal (b+) and the common negro variant (a+) of human glucose-6-phosphate dehydrogenase.
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Standardization of hemoglobinometry. II. The hemiglobincyanide method.
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GENETIC VARIATIONS IN THE QUANTITATIVE CONTROL OF ERYTHROCYTE GLUCOSE-6-PHOSPHATE DEHYDROGENASE ACTIVITY.
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Relationship between the genes for glucose-6-phosphate dehydrogenase and for haemoglobin in a Nigerian population.
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Enzymic properties of different types of human erythrocyte glucose-6-phosphate dehydrogenase, with characterization of two new genetic variants.
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Genetic variants of human erythrocyte glucose 6-phosphate dehydrogenase. II. In vitro and in vivo function of the A- variant.
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Genetic variants of human erythrocyte glucose 6-phosphate dehydrogenase. I. Regulation of activity by oxidized and reduced nicotinamide-adenine dinucleotide phosphate.
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Electrophoretic diversity of glucose-6-phosphate dehydrogenase among Greeks.
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Population genetics of haemoglobin variants, thalassaemia and glucose-6-phosphate dehydrogenase deficiency, with particular reference to the malaria hypothesis.
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Haemoglobin and glucose-6-phosphate dehydrogenase variants: distribution in relation to malaria endemicity in a Togolese population.
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