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Primary structure of myoglobin (Mb) from ordinary muscle of striped snake-head fish (Ophicephalus striatus) was studied. Sequence analysis of cloned cDNA revealed two lengths of nucleotide sequences different in 3´ untranslated regions, MbI gene and MbII gene. In accordance to amino acid coding region, both genes encoded protein with 145 amino acid residues which were different in two amino acid residues at position 114 and 117, indicating Mb isoforms. They are very close to those of various species of fish Mbs and very identical to some marine Mbs. There are amino acid differences among the fish Mbs and other Mbs that occur in the highly conserved regions in fish species. The replacement of alanine with serine 59 in fish species, adjacent to histidine 60 may contribute to the reversible binding of oxygen. Lysine was replaced by asparagine at position 93 which directly binds to the heme. The fish Mbs contain two cysteine residues. One of cysteine residue locates at the terminal of the polypeptide chain which may possibly contribute to internal disulfide interaction and thus forms tightly folded structure. It is implied that the fish Mb might be a novel protein with strong intramolecular bonding.

cDNA Sequence Analysis and Structural Phylogenetic Tree of Novel Myoglobin from Striped Snake-Head Fish (Ophicephalusstriatus)