Complete amino acid sequence of the myoglobin from the Atlantic bottlenosed dolphin, Tursiops truncatus

Abstract

The complete amino acid sequence of the major component myoglobin from the Atlantic bottlenosed dolphin, Tursiops truncatus, was determined by specific cleavage of the protein to obtain large peptides that are readily degraded by the automatic sequencer. Three easily separable peptides were obtained by cleaving the protein with cyanogen bromide at the 2 methionine residues and 4 peptides were obtained by cleaving the methyl acetimidated protein with trypsin at the 3 arginine residues. By subjecting 4 of these peptides and the apomyoglobin to automatic Edman degradation, over 80% of the covalent structure of the protein was obtained. The remainder of the primary structure was determined by further digestion of the central cyanogen bromide peptide with trypsin and staphylococcal protease. This myoglobin differs from that of the sperm whale, Physter catodon, at 15 positions, from that of the California gray whale, Eschrichtius gibbosus, at 14 positions, from that of the common porpoise, Phocoena phocoena, at 6 positions, and from the myoglobin of the Black Sea dolphin, Delphinus delphis and the Amazon River dolphin, Inia goeffrensis, at 5 and 7 positions, respecitvely. All substitutions observed in this sequence fit easily into the tertiary structure of sperm whale myoglobin.

Coordination complexes and catalytic properties of proteins and related substances. 95. Complete amino acid sequence of the myoglobin from the Dall porpoise (Phocoenoides dalli dalli) and reinvestigation of the primary structure of the myoglobin from common porpoise (Phocoena phocoena)

“…As seen in Figure 3 Dali porpoise myoglobin has close similarities in sequence with various members of the family Delphinidae (dolphins). Dali porpoise myoglobin differs in sequence by only four residues from the identical sequences of the Atlantic bottlenosed dolphin (Jones et al, 1976) and Pacific common dolphin (Wang et al, 1977) myoglobins and by six residues from the sequences of pilot whale myoglobin (Jones et al, 1978) and killer whale myoglobin (Castillo et al, 1977). The sequence of Dali porpoise myoglobin will be compared here with that of pilot whale myoglobin.…”

“…All chemical modifications, enzymatic and chemical cleavages, and peptide fractionation procedures were as described previously (Dwulet et al, 1975;Bogardt et al, 1976;Jones et al, 1978).…”

“…The remainder of the primary structure was determined by sequence analysis of tryptic peptides isolated from the central cyanogen T h i s paper reports the use of the automatic Edman degradation procedure in determining the complete amino acid sequence of the myoglobin from the Dall porpoise, Phocoenoides dalli dalli. The peptide fragmentation and the analytical procedures necessary for this determination have been established in several other cetacean myoglobin sequence papers (Dwulet et al, 1975(Dwulet et al, , 1977Bogardt et al, 1976;Jones et al, 1976Jones et al, , 1978 Lehman et al, 1977;Wang et al, 1977; DiMarchi et al, 1978). The sequence reported here differs in only two residue positions from that reported for the common porpoise, Phocoena phocoena (Bradshaw & Gurd, 1969).…”

“…The peptide fragmentation and the analytical procedures necessary for this determination have been established in several other cetacean myoglobin sequence papers (Dwulet et al, 1975(Dwulet et al, , 1977Bogardt et al, 1976;Jones et al, 1976Jones et al, , 1978Lehman et al, 1977;Wang et al, 1977;DiMarchi et al, 1978). The sequence reported here differs in only two residue positions from that reported for the common porpoise, Phocoena phocoena (Bradshaw & Gurd, 1969).…”

Coordination complexes and catalytic properties of proteins and related substances. 79. The complete amino acid sequence of the major component myoglobin of dwarf sperm whale (Kogia simus)

“…Sequenator analysis of these fragments and the apomyoglobin provided over 80% of the covalent structure of the protein. The remainder of the primary structure was determined by further In preceding papers, the complete primary structure of the myoglobins from Amazon River dolphin (Dwulet et al, 1975), California gray whale (Bogardt et al, 1976), Atlantic bottlenosed dolphin (Jones et al, 1976), and Arctic minke whale (Lehman et al, 1977) were reported. All of these sequences of cetacean myoglobins were determined by automated Edman degradation.…”