Coordination complexes and catalytic properties of proteins and related substances. 78. The complete amino acid sequence of the major component myoglobin from the Arctic minke whale, Balaenoptera acutorostrata

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Abstract
The complete primary structure of the major component myoglobin from the Arctic minke whale, B. acutorostrata, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. Over 80% of the amino acid sequence was established from the 3 peptides resulting from the cleavage of the apomyoglobin at the 2 methionine residues with CnBr along with the 4 peptides resulting from the cleavage of the methyl acetimidated apomyoglobin at the 3 arginine residues with trypsin. The further digestion of the central CnBr peptide with trypsin and Staphylococcus aureus strain V8 protease enabled the determination of the remainder of the covalent structure. This myoglobin differs from that of the dwarf sperm whale, Kogia simus, at 16 positions, and the common dolphin, Delphinus delphis, at 14 positions from that of the common porpoise, Phocaena phocaena and the bottlenosed dolphin, Tursiops truncatus, at 13 positions, from that of the Amazon River dolphin, Inia geoffrensis, at 10 positions, and from that of California gray whale, Eschrichtius gibbosus, at 3 positions. All of the substitutions observed in this sequence fit easily into the 3-dimensional structure of the sperm whale myoglobin.