Abstract
The hemoglobins of Rana catesbeiana tadpoles were resolved into five characteristic components by polyacrylamide gel electrophoresis. Characterization of the peptide chains of the major and of one other component showed each to have two types of chain, none of which is in common. The major tadpole hemoglobin with two valine NH 2-terminal groups has no peptide chain in common with the major frog hemoglobin. The latter has two chains beginning with glycine. No other amino acid groups appear to be available to the Edman end group reagent.
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