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The metabolic utilization of amino acids: potentials of 14CO2 breath test measurements

Published online by Cambridge University Press:  09 March 2007

V. V. A. M. Schreurs
Affiliation:
Department of Human and Animal Physiology, Wageningen Agricultural University, Haarweg 10, NL-6709 PJ Wageningen, The Netherlands
H. A. Boekholt
Affiliation:
Department of Human and Animal Physiology, Wageningen Agricultural University, Haarweg 10, NL-6709 PJ Wageningen, The Netherlands
R. E. Koopmanschap
Affiliation:
Department of Human and Animal Physiology, Wageningen Agricultural University, Haarweg 10, NL-6709 PJ Wageningen, The Netherlands
P. J. M. Weijs
Affiliation:
Department of Human and Animal Physiology, Wageningen Agricultural University, Haarweg 10, NL-6709 PJ Wageningen, The Netherlands
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Abstract

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The present paper offers a dual 14CO2 breath test approach to study the metabolic utilization of free amino acids in the body. Using the carboxyl-[14C]isotopomer of an amino acid as the test substrate the percentage recovery of the isotope as 14CO2 reflects which part of the labelled amino acid flux has been decarboxylated. The residual C fragments may flow to total oxidation at least to the level recovered for the universal [14C]isotopomer. In the case that recovery for total oxidation is less than for decarboxylation, part of the [14C]fragments are retained in the body by either exchange or non-oxidative pathways. Utilization of tyrosine and leucine was measured in the post-absorptive phase in adult rats conditioned on isoenergetic diets containing 210, 75 or 0 g protein/kg. It was shown that the level of dietary protein exerts an influence on both decarboxylation and total oxidation. Although the responses of leucine and tyrosine were not different for total oxidation, there was a difference between the amino acids in their relative rate of decarboxylation. That this dual 14CO2 breath test approach can be used as a tool to evaluate whether the protein and amino acid supply has been adequate to support actual requirements is discussed.

Amino acid utilization: Amino acid requirements: Leucine: Tyrosine

Type
Protein and Amino acid Metabolism
Copyright
Copyright © The Nutrition Society 1992

References

REFERENCES

Haggarty, P., Reeds, P. J., Fletcher, J. M. & Wahle, K. W. J. (1986) The fate of 14C derived from radioactively labelled dietary precursors in young rats of the Zucker strain. Biochemical Journal 235, 323327.CrossRefGoogle Scholar
Henry, Y., Arnal, M., Obled, C. & Rérat, A. (1988) Protein and amino acid requirements of pigs. In European Association for Animal Production, Symposium on Protein Metabolism and Nutrition Publication no. 35, part 3, pp. 9–18,Rostock: EAAP.Google Scholar
Millward, D. J. & Rivers, J. P. W. (1988) The nutritional role of indispensable amino acids and the metabolic basis for their requirements. European Journal of Clinical Nutrition 42, 367393.Google ScholarPubMed
Reeds, P. J. (1974) The catabolism of valine in the malnourished rat. Studies in vivo and in vitro with different labelled forms of valine. British Journal of Nutrition 31, 259270.CrossRefGoogle ScholarPubMed
Simon, O. (1989) Metabolism of proteins and amino acids. In Protein Metabolism in Farm Animals, pp. 273366 [Bock, H.D., Eggum, B. O., Low, A. G., Simon, O. and Zebrowska, T., editors]. Oxford: Oxford Science Publications.Google Scholar
Spiteri, N. J., Alingh, Prins A., Keyser, J. & Strubbe, J. H. (1982) Circadian pacemaker control of feeding in the rat, at dawn. Physiology & Behavior 29, 11411145.CrossRefGoogle ScholarPubMed
Strubbe, J. H., Keyser, J., Dijkstra, T. & Alingh, Prins A. J. (1986) Interaction between circadian and caloric control of feeding behavior in the rat. Physiology & Behavior 36, 489493.CrossRefGoogle ScholarPubMed
Stryer, L. (1988) Biochemistry, 3rd ed., pp. 373396. New York: Freeman and Co.Google Scholar
Waterlow, J. C., Garlick, P. & Millward, D. J. (1978) Protein Turnover in Mammalian Tissues and in the Whole Body. Amsterdam: North-Holland Publishing Company.Google Scholar