ISSN : 0970 - 020X, ONLINE ISSN : 2231-5039
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Abstract

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

Chatrachatchaya Chotichayapong1, Saksit Chanthai1*, Nison Sattayasai2, Nobuyuki Kanzawa3, Toru Tamiya3 and Takahide Tsuchiya3

DOI : http://dx.doi.org/10.13005/ojc/320102


Abstract:

Primary structure of myoglobin (Mb) from ordinary muscle of striped snake-head fish (Ophicephalusstriatus) was studied. Sequence analysis of cloned cDNA revealed two lengths of nucleotide sequences different in 3´ untranslated regions,MbIgene and MbII gene. In accordance to amino acid coding region, both genes encodedprotein 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 Mbsand very identical to some marine Mbs. There are amino acid differences among thefish Mbs and other Mbs that occur in the highly conserved regions infish species. The replacement of alanine with serine 59in fish species, adjacent tohistidine 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.

Keywords:

Myoglobin; Striped snake-head fish; cDNA sequence; Phylogenetic tree; Oxygen binding

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