Abstract
We investigated hemoglobin synthesis in suspension cultures of liver erythroid cells obtained from calf fetuses of 103 to 198 days. A significant amount of radioactivity was associated with adult hemoglobins which were separated from the fetal hemoglobins by isoelectric focusing, even after purification of the cell hemo-lysates by chromatography on Sephadex G-100. A radioactive β-globin fraction was isolated by chromatography on carboxymethyl-cellulose from hemolysates, which were first fractionated on Sephadex G-100. Fingerprint analysis of peptides obtained by trypsinolysis of radioactive β-globin chains revealed that its structure was closely related to that of β-globin, isolated from cow bone marrow cells. The amount of β-globin which was synthesized by calf liver cells varied from 0.3 to 3.5 % of the non-a globin chains and remained at a low level for all the fetuses which were studied. Our results indicate that the bovine fetal liver is a valuable model to investigate the switch from fetal to adult hemoglobin synthesis.