Abstract
Embryonic globin chains were found to be synthesized in vitro by the BFU-E colonies derived from adult sickle cell anemia (SS) patients, their heterozygous relatives as well as a few normal controls. In the absence of sufficient material for conducting direct structural analyses of these peptides, they were confirmed by evaluating the co-migration of the epsilon and zeta-chains with the corresponding structurally characterized globin chains obtained from K562 cell lysates on a reversed phase high performance liquid chromatogram. The presence of zeta-chain was also confirmed using an immunologic procedure. Furthermore, significant 35S-methionine incorporation peak was observed corresponding to the zeta-chain synthesized by the BFU-E-derived colonies implying an active synthesis of this embryonic globin chain in BFU-E cells obtained from hemopoietically adult persons.
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