Coordination complexes and catalytic properties of proteins and related substances. 83. Complete primary structure of the major component myoglobin of Pacific common dolphin (Delphinus delphis)

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Abstract
The complete amino acid sequence of the major component myoglobin from Pacific common dolphin, D. delphis, was determined by the automatic Edman degradation of several large peptides obtained by specific cleavages of the protein. More than 80% of the covalent structure was established by the degradation of the apomyoglobin and 5 peptides from: cyanogen bromide cleavage at the 2 methionine residues, trypsin cleavage of the acetimidated apomyoglobin at the 3 arginine residues and 2-p-nitrophenylsulfenyl-3-methyl-3''-bromoindolenine cleavage at the 2 tryptophan residues. The rest of the sequence was determined by use of the peptides prepared from further digestion of the central cyanogen bromide peptide with staphylococcal protease and trypsin. The primary structure of this myoglobin proved identical with that from the Atlantic bottlenosed dolphin, Tursiops truncatus, but showed 4 substitutions with respect to the sequence reported for the Black Sea dolphin which was given the designation D. delphis.