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Effect of food intake on hind-limb and whole-body protein metabolism in young growing sheep: chronic studies based on arterio-venous techniques

Published online by Cambridge University Press:  09 March 2007

Patricia M. Harris
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
Pat A. Skene
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
Vivien Buchan
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
E. Milne
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
A. G. Calder
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
Susan E. Anderson
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
Alexmary Connell
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
G. E. Lobley
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
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Abstract

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Whole-body protein synthesis, estimated by the irreversible loss rate procedure, and hind-leg protein metabolism determined by arterio-venous techniques were monitored in response to three nutritional conditions (approximately 0.6, 12 and 1.8 x energy maintenance (M)) in ten wether lambs (33 kg average live weight). In all lambs and treatments measurements were based on radiolabelled phenylalanine, but the terminal procedures (five at 0.6 x M and five at 1.8 x M) also included infusion of [1-13C]leucine; this permitted comparison of amino acids catabolized (leucine) and non-metabolized (phenylalanine) by the hind-limb tissues. Whole-body protein synthesis increased with intake and the relationship with energy expenditure was slightly lower than that reported previously for pigs and cattle. The efficiency of protein retention: protein synthesis did not exceed 0.25 between the two intake extremes. Effects of intake on amino acid oxidation were similar to those observed for cattle. Hind-limb protein synthesis also increased significantly (P < 0.001) in response to intake. Estimates of protein gain, from net uptake values, indicated that the tissues made a greater proportional contribution to total protein retention above M and to protein loss below M, emphasizing the role played by muscle tissue in providing mobile protein stores. The rates of protein synthesis calculated depended on the selection of precursor (blood) metabolite, but rates based on leucine always exceeded those based on phenylalanine when precursor from the same pool was selected. The incremental efficiency of protein retained: protein synthesis was apparently unity between 0.6 and 1.2 x M but 0.3 from 1.2 to 1.8 x M. Blood flow through the iliac artery was also proportional to intake. Leucine and oxo-acid catabolism to carbon dioxide increased with intake such that the metabolic fate of the amino acid was distributed in the proportion 2:1 between protein gain and oxidation. The rates of oxidation were only 1–3% the reported capacity of the rate-limiting dehydrogenase enzyme in muscle, but sufficient enzyme activity resides in the hind-limb adipose tissue to account for such catabolism

Type
Protein Digestion and Metabolism
Copyright
Copyright © The Nutrition Society 1992

References

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