Abstract

The amino acid sequences of skeletal muscle myoglobins from two old-world monkeys, Presbytis entellus and Erythrocebus patas, as well as one new-world monkey, Cebus apella were inferred by homology of the tryptic and peptic peptides with the known sequence of human myoglobin and by selective dansyl-Edman degradation. These new sequences were examined phylogenetically in conjunction with the 15 primate sequences already reported. It is clear that myoglobin evolution has been extremely conservative among cercopithecoid primates, so much so that the two surviving subfamilies cannot be distinguished using this protein.

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