The expression of fetal hemoglobin, Hb F, in the adult cells is cellularly restricted both in vivo and in culture. Because, in cultures of erythroid progenitors, subclones that express or fail to express Hb F are derived from the same erythroid stem cell, a mechanism must exist whereby Hb F expression segregates in the progeny of erythroid progenitors during their differentiation. We present ma...

KMOE -2/05 cells, derived from a patient with acute erythremia, became benzidine-positive after the addition of cytosine arabinoside (CA). Radioimmunoassays using antihuman hemoglobin antibodies revealed an elevated amount of hemoglobin in the CA-exposed cells over that in the control cells (without CA). Isoelectric focusing of the CA-exposed cell lysate formed benzidine-positive foci in the po...

Although the fetal and adult hemoglobins of many species, including man, are essentially similar in molecular weight and in spectroscopic characteristics, they exhibit marked differences in other chemical and physical properties (l-6). Therefore, they may be assumed to represent distinct chemical entities. The present study was undertaken to determine whether the chemical difference is expresse...

We have constructed a plasmid (pHE2) in which the synthetic human alpha- and beta-globin genes and the methionine aminopeptidase (Met-AP) gene from Escherichia coli are coexpressed under the control of separate tac promoters. The Hbs were expressed in E. coli JM109 and purified by fast protein liquid chromatography, producing two major components, a and b. Electrospray mass spectrometry shows t...

The existence of two adult hemoglobin types, designated as hemoglobin A (or hemoglobin II) and hemoglobin B (or hemoglobin I), in various breeds of sheep is well established (for reference see van Vliet and Huisman (1)). The two molecular species have been separated both by electrophoresis, with which hemoglobin A showed the highest mobility at alkaline pH, and by chromatography on either Amber...

The existence of two adult hemoglobin types, designated as hemoglobin A (or hemoglobin II) and hemoglobin B (or hemoglobin I), in various breeds of sheep is well established (for reference see van Vliet and Huisman (1)). The two molecular species have been separated both by electrophoresis, with which hemoglobin A showed the highest mobility at alkaline pH, and by chromatography on either Amber...