Abstract
The alpha and beta chains of White-Throated Capuchin (Cebus capucinus) hemoglobin were separated and digested by trypsin. The tryptic peptides were isolated and sequenced by conventional methods. The peptides in each chain were aligned by the homology of their sequences with those of human adult hemoglobin. The primary structures thus deduced are compared with those of other primate hemoglobins, and we discuss the molecular evolution of hemoglobins, in particular the rate of evolution in New World monkey hemoglobins.
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