Shark Myoglobins. II. Isolation, characterization and amino acid sequence of myoglobin from galeorhinus japonicus

Abstract

Native oxymyoglobin (MbO2) was isolated from red muscle of G. japonicus by chromatographic separation from metmyoglobin (metMb) on DEAE-cellulose and the amino acid sequence of the major chain was determined with the aid of sequence homology with that of G. australis. It was shown to differ in amino acid sequence from that of G. australis by 10 replacements, to be acetylated at the amino terminus and to contain glutamine at the distal (E7) residue. It was also shown to have a spectrum very similar to that of mammalian MbO2. However, the pH-dependence for the autoxidation of MbO2 was seen to be quite different from that of sperm whale (Physeter catodon) MbO2. Although the sequence homology between spermwhale and G. japonicus myoglobins is about 40%, their hydropathy profiles were very similar, indicating that they have asimilar geometry in their globin folding. © 1985 ASEG.