Diminished synthesis of an alpha chain mutant, hemoglobin I (α16 lys → glu)

Abstract

In patients heterozygous for abnormal hemoglobins there is usually less than 50% of the mutant hemoglobin present in peripheral blood. The synthetic rates of α-chain mutants compared to α^A have not been reported to date. In this study the production of α^A- and α^I-chains has been measured in peripheral blood and bone marrow of two patients with approximately 30% hemoglobin I, an α-chain abnormality (α^{16 lys → glu}). The results suggest that the decreased amount of α^I compared to α^A is due solely to diminished biosynthesis of the α^I-chains. The relative rates of synthesis of α^I- and α^A-chains are similar in both nucleated red cells and reticulocytes indicating that no change occurs during erythroid cell maturation which preferentially affects either α^I or α^A production.