Open AccessKinetic Evidence for the Existence of α‐Globin Pool in β‐Thalassemic Reticulocytes
Author(s) -
Bargellest A.,
Pontremoli S.,
Menini C.,
Conconi F.,
Melloni E.
Publication year - 1968
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1968.tb19576.x
Subject(s) - incubation , globin , cytoplasm , incubation period , biochemistry , lysis , kinetics , biology , hemoglobin , microbiology and biotechnology , chemistry , chromatography , physics , quantum mechanics
The kinetics of incorporation of 3 H‐labeled amino acids into α, β, and γ globin has been determined, following incubation of intact reticulocytes, in stroma‐free hemolysates and in purified Hb F and Hb A from homozygous β‐thalassemic subjects. The labeled globins present in the cytoplasm as well as in purified Hb F and Hb A at various incubation times, were separated by CM‐cellulose chromatography, and the ratios of [ 3 H]α to [ 3 H]counterpart globins were determined. The results obtained show that in the initial stages of incubation, the ratios of [ 3 H]α to [ 3 H]‐counterpart globins are higher than 1 in the total lysate and in purified hemoglobins; these ratios, after long periods of incubation, decrease to values below 1. These findings suggest that the excess of newly synthesized α molecules flows very rapidly from the polyribosomes to the hemoglobins, and then, more slowly, to a “stromal”α pool. A model is presented, showing the most likely mechanism for the overall process.