title: The synthesis of adult hemoglobins during hepatic erythropoiesis in the calf fetus.
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 hemolysates by chromatography on Sephadex G-100. A radioactive beta-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 beta-globin chains revealed that its structure was closely related to that of beta-globin, isolated from cow bone marrow cells. The amount of beta-globin which was synthesized by calf liver cells varied from 0.3 to 3.5% of the non-alpha 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.
mesh_terms: D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D004920:Erythropoiesis; D005319:Fetal Hemoglobin / Q000032:analysis / Q000096:biosynthesis; D005333:Fetus / Q000502:physiology*; D005914:Globins / Q000032:analysis; D006441:Hemoglobin A / Q000032:analysis / Q000096:biosynthesis*; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D008099:Liver / Q000166:cytology / Q000378:metabolism* / Q000502:physiology
chemical_list: D005914:Globins; D006441:Hemoglobin A; D005319:Fetal Hemoglobin