Advanced SearchSearch Tips
Comparison of the []Phenylalanine Model with the [1-]Leucine Method to Determine Whole Body Protein Synthesis and Degradation in Sheep Fed at Two Levels
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Comparison of the []Phenylalanine Model with the [1-]Leucine Method to Determine Whole Body Protein Synthesis and Degradation in Sheep Fed at Two Levels
Al-Mamun, M.; Ito, C.; Fujita, T.; Sano, H.; Sato, A.;
  PDF(new window)
The []phenylalanine model was compared with the [1-]leucine method to determine whole body protein synthesis (WBPS) and degradation (WBPD) in sheep fed at two levels. The animals were fed either 103 (M-diet) or 151 (H-diet) kcal once daily in a crossover design for 21 days each. The isotope dilutions were simultaneously conducted as a primed-continuous infusion of []phenylalanine, []tyrosine and [1-]leucine on each dietary treatment. The WBPS and WBPD calculated from the []phenylalanine model were lower (p = 0.009 and p = 0.003, respectively) than those calculated from the [1-]leucine method. The WBPS tended to be higher (p = 0.08) and WBPD was numerically higher (p = 0.33) for H-diet than M-diet in the []phenylalanine model, whereas the WBPS was numerically higher (p = 0.37) for H-diet and WBPS remained similar (p = 0.79) between diets in the [1-]leucine method. However, the absolute values and the directions of WBPS as well as WBPD from M-diet to H-diet were comparable between the []phenylalanine model and [1-]leucine method. Moreover, the values vary depending on the use of the respective amino acid contents in the carcass protein when calculating WBPS and WBPD. Therefore, it is concluded that the []phenylalanine model could be used as an alternative to the [1-]leucine method for the determination of WBPS and WBPD in sheep.
Isotope Dilution Method;Stable Isotope;Dietary Intake;Protein Synthesis;Protein Degradation;Sheep;
 Cited by
Intermediary Metabolism of Plasma Acetic Acid, Glucose and Protein in Sheep Fed a Rice Straw-based Diet,Alam, M.K.;Ogata, Y.;Sako, Y.;Al-Mamun, M.;Sano, H.;

Asian-Australasian Journal of Animal Sciences, 2010. vol.23. 10, pp.1333-1339 crossref(new window)
Borel, M. J., P. E. Williams, K. Jabbour, J. C. Hibbard and P. J. Flakoll. 1997. Maintaining muscle protein anabolism after a metabolic stress: role of dextrose vs. amino acid availability. Am. J. Physiol. Endocrinol. Metab. 272:E36-E44.

Bregendahl, K., L. Liu, J. P. Cant, H. S. Bayley, B. W. McBride, L. P. Milligan, J. T. Yen and M. Z. Fan. 2004. Fractional protein synthesis rates measured by an intraperitoneal injection of a flooding dose of L-[ring-2H5]phenylalanine in pigs. J. Nutr. 134:2722-2728.

Brouwer, E. 1965. Report on sub-committee on constants and factors. In: Energy Metabolism. (Ed. K. L. Blaxter). Academic Press, London. pp. 302-304.

Calder, A. G. and A. Smith. 1988. Stable isotope ratio analysis of leucine and ketoisocaproic acid in blood plasma by gas chromatography/mass spectrometry. Use of tertiary butyldimethylsilyl derivatives. Rapid Commun. Mass Spectrom. 2:14-16. crossref(new window)

Clark, S. E., C. A. Karn, J. A. Ahlrichs, J. Wang, C. A. Leitch, E. A. Leitchty and S. C. Denne. 1997. Acute changes in leucine and phenylalanine kinetics produced by parenteral nutrition in premature infants. Pediatr. Res. 41:568-574. crossref(new window)

Clarke, J. T. R. and D. M. Bier. 1982. The conversion of phenylalanine to tyrosine in man. Direct measurement by continuous intravenous tracer infusions of L-[ring-$^2H_5$]phenylalanine and L-[1-$^{13}C$]tyrosine in the post absorptive state. Metabol. 31:999-1005. crossref(new window)

Connell, A., A. G. Calder, S. E. Anderson and G. E. Lobley. 1997. Hepatic protein synthesis in sheep: effect of intake as monitored by use of stable-isotope-labelled glycine, leucine and phenylalanine. Br. J. Nutr. 77:255-271. crossref(new window)

Fujita, T., M. Kajita and H. Sano. 2007. Effects of non-protein energy intake on whole body protein synthesis, nitrogen retention and glucose turnover in goats. Asian-Aust. J. Anim. Sci. 20:536-542.

Fujita, T., M. Kajita and H. Sano. 2006. Responses of whole body protein synthesis, nitrogen retention and glucose kinetics to supplemental starch in goats. Comp. Biochem. Physiol. B. 144:180-187. crossref(new window)

Gibson, N. R., F. Jahoor, L. Ware and A. A. Jackson. 2002. Endogenous glycine and tyrosine production is maintained in adults consuming a marginal-protein diet. Am. J. Clin. Nutr. 75:511-518.

Harris, P. M., P. A. Skene, V. Buchan, E. Milne, A. G. Calder, S. E. Anderson, A. Connell and G. E. Lobley. 1992. Effect of food intake on hind-limb and whole-body protein metabolism in young growing sheep: chronic studies based on arterio-venous techniques. Br. J. Nutr. 68:389-407. crossref(new window)

Kita, K., T. Muramatsu, I. Tasaki and J. Okumura. 1989. Influence of dietary non-protein energy intake on whole-body protein turnover in chicks. Br. J. Nutr. 61:235-244. crossref(new window)

Krishnamurti, C. R. and S. M. Janssens. 1988. Determination of leucine metabolism and protein turnover in sheep, using gasliquid chromatography-mass spectrometry. Br. J. Nutr. 59:155-164. crossref(new window)

Lapierre, H., J. P. Blouin, J. F. Bernier, C. K. Reynolds, P. Dubreuil and G. E. Lobley. 2002. Effect of supply of metabolizable protein on whole body and splanchnic leucine metabolism in lactating cows. J. Dairy Sci. 85:2631-2641. crossref(new window)

Lobley, G. E., X. Shen, G. Le, D. M. Bremner, E. Milne, A. G. Calder, S. E. Anderson and N. Dennison. 2003. Oxidation of essential amino acids by the ovine gastrointestinal tract. Br. J. Nutr. 89:617-629. crossref(new window)

Marchini, J. S., L. Castillo, T. E. Chapman, J. A. Vogt, A. Ajami and V. R. Young. 1993. Phenylalanine conversion to tyrosine: comparative determination with L-[Ring-$^2H_5$]phenylalanine and L-[1-$^{13}C$]phenylalanine as tracers in man. Metabol. 42:1316-1322. crossref(new window)

Matthews, D. E., H. P. Schwarz, R. D. Yang, K. J. Motil, V. R. Young and D. M. Bier. 1982. Relationship of plasma leucine and alpha-ketoisocaproate during a L-[1-$^{13}C$]leucine infusion in man: a method for measuring human intracellular leucine tracer enrichment. Metabol. 31:1105-1112. crossref(new window)

Millward, D. J., G. M. Price, P. J. H. Pacy and D. Halliday. 1991. Whole-body protein and amino acid turnover in man: what can we measure with confidence? Proc. Nutr. Soc. 50:197-216.

National Research Council. 1985. Nutrient Requirements of Sheep. 6th rev. ed. National Academy Press, Washington, DC.

Pacy, P. J., G. M. Price, D. Halliday, M. R. Quevedo and D. J. Millward. 1994. Nitrogen homeostasis in man: the diurnal responses of protein synthesis and degradation and amino acid oxidation to diets with increasing protein intakes. Clin. Sci. 86:103-118.

Pen, B., T. Iwama, M. Ooi, T. Saitoh, K. Kida, T. Iketaki, J. Takahashi and H. Hidari. 2006. Effect of potato by-products based silage on rumen fermentation, methane production and nitrogen utilization in holstein steers. Asian-Aust. J. Anim. Sci. 19:1283-1290.

Reeds, P. J., M. F. Fuller, A. Cadenhead and G. E. Lobley. 1981. Effects of changes in the intakes of protein and non-protein energy on whole-body protein turnover in growing pigs. Br. J. Nutr. 45:539-546. crossref(new window)

Rocchiccioli, F., J. P. Leroux and P. Cartier. 1981. Quantitation of 2-ketoacids in biological fluids by gas chromatography chemical ionization mass spectrometry of o-trimethylsilylquinoxalinol derivatives. Biomed. Mass Spectrom. 8:160-164. crossref(new window)

Sano, H., M. Kajita and T. Fujita. 2004. Effect of dietary protein intake on plasma leucine flux, protein synthesis, and degradation in sheep. Comp. Biochem. Physiol. B 139:163-168. crossref(new window)

SAS. 1996. $SAS/STAT^{\circledR}$ Software: Changes and Enhancements through Release 6.11. SAS Inst. Inc. Cary, NC.

Savary-Auzeloux, I., S. O. Hoskin and G. E. Lobley. 2003. Effect of intake on whole body plasma amino acid kinetics in sheep. Reprod. Nutr. Dev. 43:117-129. crossref(new window)

Schroeder, G. F., E. C. Titgemeyer, M. S. Awawdeh, J. S. Smith and D. P. Gnad. 2006. Effects of energy level on methionine utilization by growing steers. J. Anim. Sci. 84:1497-1504.

Thompson, G. N., P. J. Pacy, H. Merritt, G. C. Ford, M. A. Read, K. N. Cheng and D. Halliday. 1989. Rapid measurement of whole body and forearm protein turnover using a [$^2H_5$]phenylalanine model. Am. J. Physiol. 256:E631-E639.

Weatherburn, M. W. 1967. Phenol-hypochloride reaction for determination of ammonia. Anal. Chem. 39:971-974. crossref(new window)

Whittaker, P. G., C. H. Lee, B. G. Cooper and R. Taylor. 1999. Evaluation of phenylalanine and tyrosine metabolism in late human pregnancy. Metabol. 48:849-852. crossref(new window)

Wolfe, R. R. 1984. Tracers in metabolic research. Radioisotope and stable isotope/mass spectrometry methods. Alan R. Liss, Inc., New York.

Young, B. A., B. Kerrigan and R. J. Christopherson. 1975. A versatile respiratory pattern analyzer for studies of energy metabolism of livestock. Can. J. Anim. Sci. 55:17-22. crossref(new window)

Zello, G. A., L. Marai, A. S. F. Tung, R. O. Ball and P. B. Pencharz. 1994. Plasma and urine enrichments following infusion of L- [1-$^{13}C$]phenylalanine and L-[ring-$^2H_5$]phenylalanine in humans: evidence for an isotope effects in renal tubular reabsorption. Metabol. 43:487-491. crossref(new window)