The primary structure of myoglobin from pacific green sea turtle (Chelonia mydas caranigra).
The amino acid sequence of the main component myoglobin from skeletal muscle of Pacific green sea turtle (Chelonia mydas caranigra) has been determined. The globin is 153 residues in length and has a free amino-terminus. The heme-binding and internal residues are as found in mammalian myoglobins. Ten substitutions are observed between this myoglobin and that from map turtle. About 38, 52, 47 and 86 substitutions are noted in comparison with the myoglobins of other reptiles, mammals, birds and fish, respectively. The inferred pattern of structural stabilization and conservation of two loci are typical of tetrapod myoglobin.
D000489:Alligators and Crocodiles; D000595:Amino Acid Sequence; D000818:Animals; D008116:Lizards; D009132:Muscles / Q000032:analysis; D009211:Myoglobin / Q000302:isolation & purification; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity; D014426:Turtles
D009211:Myoglobin; D010446:Peptide Fragments