Complete amino acid sequence of the major component myoglobin from Hubb's beaked whale, Mesoplodon carlhubbsi.

The complete primary structure of the major component myoglobin from Hubb's beaked whale, Mesoplodon carlhubbsi, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. In all experiments a Beckman 890C automatic sequencer was used to degrade the peptides. A cyanogen bromide digest was used to fragment the protein at its two methionine residues into three fragments which were separated by gel filtration. In a similar pattern the protein was citraconylated to protect the lysine residues and the modified protein fragmented at its arginine residues with trypsin. The three peptides obtained here were also purified by gel filtration. Sequencer analysis of the whole apoprotein, cyanogen bromide fragments and the peptides cleaved at the arginine residues with trypsin provided 80% of the completed sequence. The remainder of the sequence was obtained by digesting the middle cyanogen bromide fragment with staphylococcal protease and by total tryptic digestion of the whole apoprotein and isolating the resulting peptides by ion-exchange chromatography. The primary structure of the Mesoplodon carlhubbsi myoglobin represents a sequence which may be closey related to the ancestral sequence of all cetacean myoglobins.