The amino acid sequence of alligator (Alligator mississippiensis) myoglobin. Phylogenetic implications

Abstract

The amino acid sequence of myoglobin from cardiac muscle of the American alligator (Alligator mississippiensis) was established by alignment of overlapping peptides and dansyl-Edman degradation. The chain initiating methonine seems to be retained. Thus, this molecule has 154 amino acid residues rather than 153 as in other tetrapod myoglobins. Maximum parsimony analysis indicated that alligator myoglobin diverges more from both bird and mammal myoglobins than these latter do from each other. The phylogenetic implications are discussed with respect to a possible diphyletic origin for diapsid reptiles.