Amino acid sequence of myoglobin from the mollusc Bursatella leachii

The complete amino acid sequence of myoglobin from the triturative stomach of gastropodic mollusc Bursatella leachii has been determined. It is composed of 146 amino acid residues, is acetylated at the N-terminus, and contains a single histidine residue at position 95 which corresponds to the heme-binding proximal histidine. The E7 distal histidine, which is conserved widely in myoglobins and hemoglobins, is replaced by valine in Bursatella myoglobin. The amino acid sequence of Bursatella myoglobin shows strong homology (73-84%) with those of Aplysia and Dolabella myoglobins.