Coordination complexes and catalytic properties of proteins and related substances. 94. Complete amino acid sequence of myoglobin from the pilot whale, Globicephala melaena

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Abstract
The complete amino acid sequence of the major compnent myoglobin from the pilot whale, Globicephala melaena, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. The apomyoglobin was selectively cleaved at the 2 methionyl residues with cyanogen bromide and the acetimidated apomyoglobin was cleaved at the 3 arginyl residues by trypsin. From the sequence analysis of 4 of these peptides and the apoprotein, over 90% of the covalent structure of the protein was obtained. The remainder of the primary structure was determined by sequence analysis of 3 of the tryptic peptides isolated from the central cyanogen bromide fragment after modification of its single arginyl residue with 1,2-cyclohexanedione. This myoglobin differs from that of the Black Sea dolphin at 4 positions and from the myoglobin of the killer whale, Pacific common dolphin and Atlantic bottlenosed dolphin at 2 positions. The above differences reflect the close taxonomic relationship of these 5 spp. of Cetacea. This sequence determination was aided by the use of a Texas Instruments 980A minicomputer system which performed peak integrations for all samples subjected to amino acid analysis.

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