Research Article| Volume 76, ISSUE 4, P616-621, October 1970

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Globin chain synthesis in heterozygotes for beta chain mutations

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      There is less abnormal hemoglobin compared to hemoglobin A (HbA) in the peripheral blood of most patients heterozygous for the production of mutant β-globin chains although, theoretically, each of the 2 β-chain genes should direct the synthesis of equal amounts of β-chains. To investigate this problem, the rates of synthesis of sickle β-chains (β6 glu → val) and Riverdale-Bronx (RB) β-chains (β24 gly → arg) have been compared to that of normal βA-chains in the reticulocytes of these patients. Previous studies of the patient with hemoglobin RB measured incorporation into isolated hemoglobins and suggested that hemoglobins A and RB are synthesized at similar rates. In the interpretation of these experiments, it was assumed that there is equal incorporation of radioactivity into the α- and β-chains. In the experiments reported here, total globin chain synthesis was measured more directly by quantitating incorporation of radioactivity into globin chains in unfractionated stroma-free hemolysates in peripheral blood. The data indicate that βRB is synthesized at a diminished rate compared to that of βA. Similar studies in patients with sickle-cell trait indicate that the rate of synthesis of βS-chains is decreased compared to that of βA-chains.
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