Amino and fatty acid profiles of wild-sourced grouper (Epinephelus coioides) broodstock and larvae
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This study was undertaken to provide information on the levels of amino acids in the muscle, liver and gonad of wild-sourced broodstock and larvae, as well as in neurula eggs and day 35 larvae from a hatchery. The fatty acid composition of grouper broodstock tissues was also determined. Samples were analysed for crude protein, amino acids, total lipids and fatty acid contents. Muscle contained higher levels of crude protein and amino acids than the ovary and liver. At the early maturing stage, the grouper ovarian protein was 73.3% and lipid was 19.3%, indicating the high dietary requirements of these nutrients for ovarian development. The crude protein and amino acid contents in wild-sourced larvae were higher than that in eggs and larvae from the hatchery.
Alava, V. R., Priolo, F. M. P., Arnaiz, M., & Toledo, J. D. (2004). Amino and fatty acid profiles of wild-sourced grouper (Epinephelus coioides) broodstock and larvae. In S. McBride & K. C. Williams (Eds.), Advances in grouper aquaculture (pp. 53–54). Canberra: Australian Centre for International Agricultural Research.
PublisherAustralian Centre for International Agricultural Research
SeriesACIAR Monograph 110
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Molecular cloning and localization of GABAA receptor-associated protein in the rotifer Brachionus plicatilis HS Marcial, K Suga, S Kinoshita, G Kaneko, A Hagiwara & S Watabe -
International Review of Hydrobiology, 2014 - Wiley-VCH Verlagγ-Aminobutyric acid receptor type A-associated protein (GABARAP) and its homologs constitute a protein family found in many eukaryotes from yeast to human, and are known to be involved in intracellular membrane trafficking of GABAA receptors and autophagy. In this study, we cloned cDNA-encoding GABARAP from the monogonont rotifer Brachionus plicatilis and examined for its tissue distribution at the protein level in neonates, males and females. Using reverse transcription (RT)-PCR and rapid amplification of cDNA ends (RACE) techniques, we showed that like other GABARAPs, rotifer GABARAP was also composed of 117 amino acids and highly homologous to vertebrate GABARAP2 ortholog (74–76% identity). GABARAP was demonstrated with its specific antibody to be ubiquitously distributed, irrespective of neonates, males, and females, in the coronal area that covers brain and contains most mechano- and chemoreceptors. Rotifer GABARAP was also expressed in the mature eggs but not in immature eggs. Double immunostaining with mammalian anti-GABA γ receptor antibody showed that rotifer GABARAP co-localized with GABA receptor, suggesting the association of the two proteins. The presence of GABARAP in rotifer implies that it is highly conserved during evolution, and plays important roles in various biological processes.
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