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Is the trimodality of Hb leslie (α 2 β 2 131 Gln → 0) in heterozygotes the result of a variable number of active α‐chain genes? Evidence for posttranslational control of hemoglobin synthesis
Author(s) -
Felice A.,
Abraham E. C.,
Miller A.,
Stallings M.,
Huisman T. H. J.
Publication year - 1978
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830050102
Subject(s) - genetics , gene , heterozygote advantage , chain (unit) , biology , physics , allele , astronomy
Whether the trimodality in the relative concentration of the hemoglobin variant Hb Leslie in heterozygotes (Huisman, Hemoglobin 1: 349–382, 1977) is due to a polymorphism of the α‐chain structural genes was investigated by conventional incubation of reticulocytes with 14 C‐leucine. In addition, an aliquot from each of the incubations was incubated under the same conditions but without isotope. Three Hb Leslie heterozygotes with presumably four, three (heterozygous α‐thalassemia‐2), and two (homozygous α‐thalassemia‐2) active α‐chain genes and with 33%, 22%, and 11% Hb Leslie respectively, and one patient with the Hb Leslie β 0 ‐thalassemia condition with more than 85% Hb Leslie were studied. The data indicate that β Leslie chains have a lower affinity for α chains than β A chains. A concomitant α‐chain deficiency results in a reduced incorporation of β Leslie chains into the tetrameric Hb Leslie molecules, while the quantity of Hb Leslie produced correlates with the degree of α‐chain deficiency. Excess of β Leslie chains is preferentially degraded.