For what its worth.
Oxidation of glutamine by the splanchnic bed in humans.
Haisch M, Fukagawa NK, Matthews DE.
Departments of Medicine and Chemistry, University of Vermont, Burlington, Vermont 05405, USA.
[1,2-(13)C(2)]glutamine and [ring-(2)H(5)]phenylalanine were infused for 7 h into five postabsorptive healthy subjects on two occasions. On one occasion, the tracers were infused intravenously for 3.5 h and then by a nasogastric tube for 3.5 h. The order of infusion was reversed on the other occasion. From the plasma tracer enrichment measurements at plateau during the intravenous and nasogastric infusion periods, we determined that 27 +/- 2% of the enterally delivered phenylalanine and 64 +/- 2% of the glutamine were removed on the first pass by the splanchnic bed. Glutamine flux was 303 +/- 8 micromol. kg(-1). h(-1). Of the enterally delivered [(13)C]glutamine tracer, 73 +/- 2% was recovered as exhaled CO(2) compared with 58 +/- 1% of the intravenously infused tracer. The fraction of the enterally delivered tracer that was oxidized specifically on the first pass by the splanchnic bed was 53 +/- 2%, comprising 83% of the total tracer extracted. From the appearance of (13)C in plasma glucose, we estimated that 7 and 10% of the intravenously and nasogastrically infused glutamine tracers, respectively, were converted to glucose. The results for glutamine flux and first-pass extraction were similar to our previously reported values when a [2-(15)N]glutamine tracer [Matthews DE, Morano MA, and Campbell RG, Am J Physiol Endocrinol Metab 264: E848-E854, 1993] was used. The results of [(13)C]glutamine tracer disposal demonstrate that the major fate of enteral glutamine extraction is for oxidation and that only a minor portion is used for gluconeogenesis.
Splanchnic bed utilization of glutamine and glutamic acid in humans.
Matthews DE, Marano MA, Campbell RG.
Department of Medicine, Cornell University Medical College, New York, New York 10021.
To study the fate of enterally delivered nonessential amino acids, glutamine and glutamate, 14 healthy adults were infused in the postabsorptive state with [2-15N]glutamine and [15N]glutamate for 7 h by intravenous (iv) and nasogastric (ng) tube routes. The amount of enterally delivered tracer that was sequestered by the splanchnic bed on the first pass was 54 +/- 4 and 88 +/- 2% for the [2-15N]glutamine and [15N]glutamate tracers, respectively. Only 46 and 12% of the ng glutamine and glutamate tracers entered systemic blood, respectively. The relative amount of 15N transferred from glutamate to glutamine, the transaminating amino acids leucine, isoleucine, valine, and alanine, and to proline was significantly higher when the [15N]glutamate was infused by the ng vs. iv route. The same was also true for [2-15N]glutamine, which presumably transferred 15N after it was converted to glutamate. Thus we conclude that the splanchnic bed sequesters over one-half of the glutamine and almost all of the glutamate delivered to it in the postabsorptive state. There is production of transaminating amino acids in the splanchnic bed, and the splanchnic bed produces simultaneously both glutamine from glutamate and glutamate from glutamine.
For those that think peptides are better, I believe this is the only one comparing the two.
Free and protein-bound glutamine have identical splanchnic extraction in healthy human volunteers.
Boza JJ, Dangin M, Moennoz D, Montigon F, Vuichoud J, Jarret A, Pouteau E, Gremaud G, Oguey-Araymon S, Courtois D, Woupeyi A, Finot PA, Ballevre O.
Nestle Research Center, Vers-Chez-Les-Blanc, 1000 Lausanne 26, Switzerland.
The objectives of the present study were to determine the splanchnic extraction of glutamine after ingestion of glutamine-rich protein ((15)N-labeled oat proteins) and to compare it with that of free glutamine and to determine de novo glutamine synthesis before and after glutamine consumption. Eight healthy adults were infused intravenously in the postabsorptive state with L-[1-(13)C]glutamine (3 micromol x kg(-1) x h(-1)) and L-[1-(13)C]lysine (1.5 micromol x kg(-1) x h(-1)) for 8 h. Four hours after the beginning of the infusion, subjects consumed (every 20 min) a liquid formula providing either 2.5 g of protein from (15)N-labeled oat proteins or a mixture of free amino acids that mimicked the oat-amino acid profile and contained L-[2,5-(15)N(2)]glutamine and L-[2-(15)N]lysine. Splanchnic extraction of glutamine reached 62.5 +/- 5.0% and 66.7 +/- 3.9% after administration of (15)N-labeled oat proteins and the mixture of free amino acids, respectively. Lysine splanchnic extraction was also not different (40.9 +/- 11.9% and 34.9 +/- 10.6% for (15)N-labeled oat proteins and free amino acids, respectively). The main conclusion of the present study is that glutamine is equally bioavailable when given enterally as a free amino acid and when protein bound. Therefore, and taking into consideration the drawbacks of free glutamine supplementation of ready-to-use formulas for enteral nutrition, protein sources naturally rich in this amino acid are the best option for providing stable glutamine.
