Submitted to: Annual Eastern Fish Health Workshop
Publication Type: Abstract Only
Publication Acceptance Date: March 10, 2007
Publication Date: May 16, 2007
Citation: Gaylord, T.G., Overturf, K.E., Barrows, F., Teague, A.M., Snyder, S.G. 2007. Protein turnover: validation of a stable isotope flooding dose technique and potential utilization for nutrition based in a selective breeding program.. Book of Abstracts World Aquaculture Society. Technical Abstract: Protein growth is a key concern in trout productions systems. The ability to develop diets for maximal protein accretion efficiency has multiple benefits, including reduced production cost and reduced nitrogenous waste loads. Along with improve diets developed for maximized protein accretion efficiency, production of fish genetically selected for improved growth and protein accretion efficiencies will have similar economic and environmental benefits. In order to address protein growth efficiencies due to diet and selective breeding, the ability to quantify protein turnover is crucial. Protein turnover is the difference between protein synthesis rates and protein degradation rates. Quantification of these two counteracting processes has been difficult. Protein synthesis has been measured utilizing the flooding dose technique with radio-labeled phenylalanine as a tracer. Protein degradation has most often been measured over a longer period of time (days) by difference between protein accretion and protein synthesis. In order to measure protein synthesis and degradation over similar timeframes, it is necessary to find suitable tracers that can be used to pre-label proteins in conjunction with the flooding dose technique that may be used to quantify protein synthesis and degradation in specific tissues. Also, validation of an in vivo time course to meet the basic assumption of the flooding dose technique will have to be established. The presentation will discuss the difficulties encountered with measuring protein synthesis and degradation simultaneously and the utilization of stable isotopes with LC-MS detection. Potential areas of application also will be discussed.