Ubiquitous distribution of fluorescent protein in muscles of four species and two subspecies of eel (genus Anguilla) |
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Authors: | AKI FUNAHASHI TAKAO ITAKURA ABEER A. I. HASSANIN MASAHARU KOMATSU SEIICHI HAYASHI YOSHIO KAMINISHI |
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Affiliation: | 1.Faculty of Fisheries,Kagoshima University,Kagoshima,Japan;2.Faculty of Veterinary Medicine, Department of Animal Wealth,Suez Canal University,Ismailia,Egypt;3.Fish Farming and Technology Institute,Suez Canal University,Ismailia,Egypt |
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Abstract: | In this study, the localization of fluorescent protein (FP) was characterized in the muscles of four species and two subspecies of eels Anguilla anguilla, A. australis, A. bicolor bicolor (b.), A. bicolor pacifica (p.) and A. mossambica in addition to the previously reported A. japonica. The open reading frame of each eel FP was 417 bp encoding 139 amino acid residues. The deduced amino acid sequences among the four species and two subspecies exhibited 91.4–100% identity, and belonged to the fatty-acid-binding protein (FABP) family. The gene structure of eel FPs in A. japonica, A. anguilla, A. australis, A. bicolor b., A. bicolor p. and A. mossambica have four exons and three introns, and were common to that of FABP family. The apo eel FPs expressed by Escherichia coli with recombinant eel FP genes were analysed for the fluorescent properties in the presence of bilirubin. The excitation and emission spectra of holo eel FPs had the maximum wavelengths of 490–496 and 527–530 nm, respectively. The holo eel FPs indicated that the fluorescent intensities were stronger in A. japonica and A. bicolor than in A. mossambica, A. australis and A. anguilla. The comparison of amino acid sequences revealed two common substitutions in A. mossambica, A. australis and A. anguilla with weak fluorescent intensity. |
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