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Lysine utilization by growing pigs: simultaneous measurement of protein accretion and lysine oxidation

Published online by Cambridge University Press:  09 March 2007

Beatrix Mnilk
Affiliation:
The Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
C. Ian Harris
Affiliation:
The Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
Malcolm F. Fuller
Affiliation:
The Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB
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Abstract

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Nitrogen retention and lysine oxidation were measured in growing pigs given diets which supplied 0, 0·2 or 0·8 of the lysine requirement, with other amino acids in relative excess. Eight groups of three female littermate pigs were used: one of each group was given each of the three diets. In half the pigs (four groups) N retention was measured at body weights (W) of approximately 25,35 and 45 kg. The other four littermate groups of three pigs were given the same three diets; when they reached 35 kg W they were given a continuous (6h) primed infusion of L-[6-3H]lysine. Lysine oxidation was estimated from the production of tritiated water. Rates of both N retention and lysine oxidation increased significantly with lysine intake; mean values (g/kg W0·75 per d) for the three diets respectively were for N retention, 0·00, 0·32 and 1·22, and for lysine oxidation 0·051, 0·058 and 0·078. From the N balance results (assuming a constant lysine concentration in body protein) the efficiency of utilization of absorbed lysine was estimated to be 0·85; from the oxidation results (assuming lysine absorbed but not retained is oxidized) the estimate was 0·95.

Type
Amino acid metabolism
Copyright
Copyright © The Nutrition Society 1996

References

REFERENCES

Association of the Official Analytical Chemists (1984). Official Methods of Analysis, 14th ed., p. 434 [Williams, S. editor]. Virginia: Association of the Official Analytical Chemists.Google Scholar
Batterham, E. S., Andersen, L. M., Baigent, D. R. & White, E. (1990). Utilization of ileal digestible amino acids by growing pigs: effect of dietary lysine concentration on efficiency of lysine retention. British Journal of Nutrition 64, 8194.CrossRefGoogle ScholarPubMed
Beckett, P. R. (1989). Amino acid oxidation. PhD Thesis, University of Aberdeen.Google Scholar
Beckett, P. R., Cadenhead, A. & Fuller, M. F. (1992). Valine oxidation: the synthesis and evaluation of L-(3-8H) Valine as a tracer in vivo. British Journal Nutrition 68, 139151.CrossRefGoogle Scholar
Bender, A. E. (1960). Corre!ation of amino acid composition with nutritive value of proteins. Clinica Chimica Acta 5, 15.CrossRefGoogle Scholar
Chen, R. F., Scott, C. & Trepman, E. (1979). Fluorescence properties of o-phthaldialdehyde derivatives of amino acids. Biochimica et Biophysica Acta 576, 440455.CrossRefGoogle ScholarPubMed
Chu, S.-H. W. & Hegsted, D. M. (1976). Adaptive response of lysine and threonine degrading enzymes in adult rats. Journal of Nutrition 106, 10891096.CrossRefGoogle ScholarPubMed
Church, F. C., Porter, D. H., Catignani, G. L. & Swaisgood, H. E. (1985). An o-phthalaldehyde spectro photometric assay for proteinases. Analytical Biochemistry 146, 343348.CrossRefGoogle Scholar
Davidson, J., Matheson, J. & Boyne, A. W. (1970). The use of automation in determining nitrogen by the Kjeldahl method, with final calculation by computer. Analyst 95, 181193.CrossRefGoogle ScholarPubMed
Fuller, M. F. (1991). Present knowledge of amino acid requirements for maintenance and production: non-ruminants. In Protein Metabolism and Nutrition. European Association of Animal Production Publication no. 59, pp. 116126 [Eggum, B. O., Boisen, S., Børsting, C., Danfær, A. and Hvelplund, T. editors]. Tjele, Denmark: National Institute of Animal Science.Google Scholar
Fuller, M. F., Cadenhead, A., Mollison, G. & Seve, B. (1987). Effects of the amount and quality of dietary protein on nitrogen metabolism and heat production in growing pigs. British Journal of Nutrition 58, 277285.CrossRefGoogle ScholarPubMed
Fuller, M. F., McWilliam, R., Wang, T. C. & Giles, L. R. (1989). The optimum dietary amino acid pattern for growing pigs. 2. Requirements for maintenance and for tissue protein accretion. British Journal of Nutrition 62, 255267.CrossRefGoogle ScholarPubMed
Gahl, M. J., Crenshaw, T. D. & Benevenga, N. J. (1992). Amino acid composition in growing pigs fed graded levels of lysine. In Proceedings of the American Society of Animal Science, p. 66. Des Moines, IA: American Society of Animal Science.Google Scholar
Goodno, C. C., Swaisgood, H. E. & Catignani, G. L. (1981). A fluorimetric assay for available lysine in proteins. Analytical Biochemistry 115, 203211.CrossRefGoogle ScholarPubMed
Langer, S. & Fuller, M. F. (1995). Lysine utilization in growing pigs at three different levels of protein. Proceedings of the Nutrition Society 54, 64A.Google Scholar
Markovitz, P. J. & Chuang, D. T. (1987). The bifunctional aminoadipic semialdehyde synthase in lysine degradation. Journal of Biological Chemistry 262, 93539358.CrossRefGoogle ScholarPubMed
Moore, S. (1963). On the determination of cystine and cysteic acid. Journal of Biological Chemistry 238, 235237.CrossRefGoogle Scholar
Nicholas, G. A., Lobley, G. E. & Harris, C. I. (1977). Use of the constant infusion technique for measuring rates of protein synthesis in the New Zealand White rabbit. British Journal of Nutrition 38, 117.CrossRefGoogle ScholarPubMed
Roth, M. (1971). Fluorescence reaction for amino acids. Analytical Chemistry 43, 880882.CrossRefGoogle ScholarPubMed
Roth, M. & Hampaï, A. (1973). Column chromatography of amino acids with fluorescence detection. Journal of Chromatography 83, 353356.CrossRefGoogle ScholarPubMed
Rowlett, R. & Murphy, J. (1981). A convenient spectrophotometric method for the kinetic analysis of the enzymatic hydrolysis of N-acyl peptides using phthaldialdehyde. Analytical Biochemistry 112, 163169.CrossRefGoogle ScholarPubMed
Spackman, D. H., Stein, W. H. & Moore, S. (1958). Chromatography of amino acids on sulphated polystyrene resins. Analytical Chemistry 30, 11851190.Google Scholar
Švedas, V.-J. K., Galaev, I. J., Borisov, I. L. & Berezin, I. V. (1980). The interaction of amino acids with o-phthaldialdehyde: a kinetic study and spectrophotometric assay of the reaction product. Analytical Biochemistry 101, 188195.CrossRefGoogle ScholarPubMed
Torrallardona, D., Harris, C. I., Milne, E. & Fuller, M. F. (1993). Contribution of intestinal microflora to lysine requirements in nonruminants. Proceedings of the Nutrition Society 52, 153A.Google Scholar
Torrallardona, D., Harris, C. I., Milne, E. & Fuller, M. F. (1994). The contribution of intestinal microflora to amino acid requirements in pigs. In Proceedings of the VIth International Symposium on Digestive Physiology in Pigs. European Association of Animal Production Publication no. 80, pp. 245–248 [Souffrant, W. B. and Hagemeister, H. editors]. Dummerstorf: FBN.Google Scholar
Torrallardona, D., Harris, C. I., Milne, E. & Fuller, M. F. (1995). Site of absorption of lysine synthesis by the gastrointestinal microflora of pigs. In Proceedings of the VII Symposium on Protein Metabolism and Nutrition,Portugal (In the press).Google Scholar
Wang, T. C. & Fuller, M. F. (1989). The optimum dietary amino acid pattern for growing pigs. 1. Experiments by amino acid deletion. British Journal of Nutrition 62, 7789.CrossRefGoogle ScholarPubMed
Wong, W. W., Lee, L. S. & Klein, P. D. (1987). Deuterium and oxygen-18 measurements on microliter samples of urine, plasma, saliva, and human milk. American Journal of Clinical Nutrition 45, 905913.CrossRefGoogle ScholarPubMed
Yamashita, K. & Ashida, K. (1969). Lysine metabolism in rats fed lysine-free diet. Journal of Nutrition 99, 267273.CrossRefGoogle ScholarPubMed