Abstract
Hemoglobin synthesized in vitro by red blood cells of thyroxine-treated Rana catesbeiana tadpoles is shown to be identical to adult frog hemoglobin by Sephadex gel filtration, by polyacrylamide gel electrophoresis of hemoglobin and of aminoethylated globin chains, and by fingerprinting of tryptic digests. The cells responsible for the synthesis of the adult hemoglobin were identified by radioautography and could be distinguished from the red cells of non-metamorphosing tadpoles by their rounder shape, relatively larger nuclei and lower content of hemoglobin. Polyacrylamide gel electrophoresis of hemoglobin and globin polypeptide chains was also used to determine the stage at which a switch in hemoglobin synthesis occurred during natural metamorphosis.
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