The essential nutrients: Proteins and amino acids
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This section aims to teach the reader the ten essential amino acids required by fish and their chemical structures, distinguish between essential and non-essential amino acids; the fate of absorbed amino acids in fish; effects of deficiencies and excesses of dietary amino acids in fish diets; the procedure on how to determine the qualitative and quantitative amino acid requirements of fish; methods of evaluating protein quality; and how to determine protein requirements of some aquaculture species.
Millamena, O. M. (2002). The essential nutrients: Proteins and amino acids. In O. M. Millamena, R. M. Coloso, & F. P. Pascual (Eds.), Nutrition in Tropical Aquaculture: Essentials of fish nutrition, feeds, and feeding of tropical aquatic species (pp. 7–20). Tigbauan, Iloilo, Philippines: Aquaculture Department, Southeast Asian Fisheries Development Center. http://hdl.handle.net/10862/3310
- Amino acids
- Classification of amino acids
- Essential amino acids
- Non-essential amino acids
- Classification of proteins
- Protein structure
- Fate of absorbed amino acids
- Importance of amino acid profiles in fish nutrition
- Qualitative amino acid requirements
- Quantitative amino acid requirements
- Deficiencies and excesses of dietary amino acids
- Evaluation of protein quality
- Protein requirement
- Guide questions
PublisherAquaculture Department, Southeast Asian Fisheries Development Center
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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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