Structural and autooxidation profiles of myoglobins from three species and one hybrid of tilapia (Cichlidae, Perciformes)

cDNAs encoding myoglobin were cloned from the slow skeletal muscles of three representative species of tilapia, namely, Nile tilapia Oreochromis niloticus, blue tilapia O. aureus, Mozambique tilapia O. mossambicus and one hybrid O. niloticus ♀ × O. aureus ♂, and the primary structures were deduced. All cDNAs contained an open reading frame of 444 base pairs, encoding 147 amino acids. The amino acid sequences of Mb were completely conserved among these species, though species variations in the nucleotide sequences were recognized both in coding and non-coding regions. The amino acid sequence identity was around 70-80% compared to other teleostean Mbs. In comparison of each α-helical segment (A through H) and the intersegment regions to the counterparts of tuna myoglobin, the α-helical segments C and F as well as the intersegment regions F-G and G-H were identical. The identities of α-helical segments B and H and the intersegment region F-G were relatively low. Differences were also recognized in the hydropathy plot and the tertiary structures obtained by homology modeling. The autooxidation rates at 25 °C of myoglobin fraction from the slow skeletal muscle were essentially the same among the above tilapia species, as expected from the conserved amino acid sequences.