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V R Young

Publications and source records attributed to V R Young.

At least 37 records · Page 2Linked to original sources
PubMed2000

Proteins, peptides and amino acids in enteral nutrition: overview and some research challenges.

We have selectively reviewed various aspects of protein and amino acid metabolism and nutrition which we feel are relevant and important in any comprehensive consideration of proteins, peptides, and amino acids in enteral nutrition. These, together with various clinical aspects of the problem that we have not addressed, are covered in more specific detail elsewhere in this volume. Our hope is that by the time this workshop is at an end a reasonable picture of the state of the art will emerge in terms of an understanding of the physiology and biochemistry of protein, peptide, and amino acids in enteral nutrition. Simultaneously, we will need to know, through careful clinical investigation, how this knowledge can best be exploited for optimizing the design of the protein/peptide/amino acid component of enteral nutrition formulations. In doing so it should be possible to achieve a more effective enteral use of proteins, peptides, and amino acids in the comprehensive clinical management of individuals under various pathophysiological states.

Amino Acids↗
PubMed2000

Arginine, citrulline, and nitric oxide metabolism in end-stage renal disease patients.

The kidneys are thought to be a major site of net de novo arginine synthesis, but the quantitative status of arginine metabolism and its substrate precursor relationship to nitric oxide (NO) synthesis in end stage renal disease (ESRD) patients have not been characterized. We have investigated kinetic aspects of whole body arginine metabolism in six patients with ESRD. They received two pre- and two post-hemodialysis intravenous tracer infusion studies with L-[guanidino-(15)N(2)]arginine and L-[(13)C]leucine during the first study, and L-[5-(13)C]arginine and L-[5-(13)C-ureido,5,5, (2)H(2)]citrulline during the second study. Arginine homeostasis in ESRD patients was found to be associated with a lower rate of arginine oxidation, and despite the decrease in renal function, the rate of de novo arginine synthesis appeared to be preserved. Plasma citrulline concentrations and flux were also elevated in these subjects compared with healthy adults. The rate of whole body NO synthesis was increased in the ESRD patients, but apparently not different pre- and post-hemodialysis therapy. The anatomic site(s) responsible for the maintenance of net de novo arginine synthesis and for the elevated NO synthesis and its pathophysiological importance in ESRD remain to be established.

Adult↗
PubMed1999

Leucine kinetics in reference to the effect of the feeding mode as three discrete meals.

In a recent study, we observed that the 24-hour leucine oxidation measured when three equal meals providing a generous intake of leucine (approximately 90 mg x kg(-1) x d(-1)) are eaten during the day is 16% lower (P < .01) than that for the same diet given as 10 hourly, equal meals. We hypothesized that the pattern of meal intake at a lower level of dietary leucine would affect the 24-hour rate of leucine oxidation and possibly improve the retention of dietary leucine. A total of 11 healthy adults participated in this investigation. The daily leucine intake was 182 micromol x kg(-1) x d(-1) (38 mg x kg(-1) x d(-1)) given with an L-amino acid diet. All subjects received three discrete meals daily for 6 days prior to a 24-hour intravenous (IV) tracer infusion of L-[1-13C]-leucine on day 7 (study 1). Four of these subjects participated in two additional studies of similar design. Study 2 involved giving [1-13C]-leucine as a constant IV infusion together with tracer added to the amino acid mixture at each meal time. In study 3, subjects received the three meals with added [1-13C]-leucine tracer while [2H3]-leucine was given as a constant IV infusion. Total leucine oxidation in studies 1 and 2 was 238+/-66 and 231+/-85 micromol x kg(-1) x d(-1), respectively. Leucine balance was positive, amounting to 18% of the total (diet + tracer) intake. The estimated mean nitrogen balance was +8 mg x kg(-1) x d(-1). Leucine oxidation was higher (P < .01) for breakfast than for the lunch meal. This difference was associated with lower insulin and higher plasma leucine concentrations at breakfast versus lunch periods. The results from study 3 suggest that the higher rate of leucine oxidation observed at breakfast as compared with lunch is not due to a difference in the immediate splanchnic fate of absorbed leucine from each meal. In comparison to our previous small frequent-meal studies, the pattern of meal feeding influences overall leucine utilization at both generous and limiting leucine intakes. Hence, it is possible that the pattern of meal feeding may affect estimations of amino acid requirements using the tracer-balance approach. Longer-term dietary studies will be needed to establish whether and the extent to which this is so.

Adult↗
PubMed1999

The Rudolf Schoenheimer Centenary Lecture. Isotopes in nutrition research.

The present lecture begins with a brief overview of the professional and scientific journey taken by Rudolf Schoenheimer, before turning to a discussion of the power of isotopic tracers in nutrition research. Schoenheimer's remarkable contributions to the study of intermediary metabolism and the turnover of body constituents, based initially on compounds tagged with 2H and later with 15N, spanned a mere decade. It is difficult, however, to overestimate the enormous impact of Schoenheimer's research on the evolution of biological science. After a relative hiatus, following Schoenheimer's death in 1941, in the use of stable nuclides as tracers in metabolism and nutrition, especially in human subjects, there is now an expanded and exciting range of techniques, experimental protocols and stable-isotope tracer compounds that are helping to probe the dynamic aspects of the metabolism of the major energy-yielding substrates, amino acids and other N-containing compounds, vitamins and mineral elements in human subjects. Various aspects of the contemporary applications of these tracers in nutrition research are covered in the present lecture.

Animals↗
PubMed1999

A tracer investigation of obligatory oxidative amino acid losses in healthy, young adults.

BACKGROUND: Estimation of the minimum requirement for indispensable amino acids (IAAs) has been attempted by assuming that obligatory oxidative losses (OOLs) of IAAs can be approximated from nitrogen losses and that the efficiency of utilization of IAAs at requirement intakes is approximately 70%. OBJECTIVE: We wished to determine the rates of OOLs in healthy adults, using L-[1-(13)C]leucine and L-[1-(13)C, methyl-(2)H(3)]methio-nine as tracers, after adjustment to a protein-free diet and how these rates compare with those when either sulfur amino acids (SAAs: methionine and cyst(e)ine) or leucine were removed from an otherwise adequate diet. DESIGN: Eleven subjects were randomly assigned to a 5-d protein-free diet or a 5-d diet providing adequate nitrogen and amino acids except for the SAAs or leucine. A 24-h constant intravenous infusion of [(15)N, (15)N]urea and L-[1-(13)C]leucine (Leu group; n = 5) or L-[1-(13)C, methyl-(2)H(3)]methionine (Met group; n = 6 ) began at 1800 on day 5 and rates of amino acid oxidation were determined. RESULTS: Mean (+/-SD) oxidation rates (mg kg(-)(1) d(-)(1)) of methionine and leucine were 6.4 +/- 1.4 and 24.7 +/- 3.6, respectively, with the protein-free diet; rates were significantly lower (3.9 +/- 2.2 and 7. 2 +/- 3.4, respectively) after the SAA- and leucine-free diets. Urea production was significantly lower (P < 0.01) with the protein-free than with the SAA- or leucine-free diet. CONCLUSIONS: Isotopically determined OOLs for methionine and leucine are consistent with losses predicted from nitrogen excretion, and consistent with our previous measurements of cysteine oxidation as an index of total SAA losses. The data further support our earlier conclusions regarding methionine sparing by cysteine and tentative recommended SAA requirements in adults.

Adult↗
PubMed1999

Incorporation of urea and ammonia nitrogen into ileal and fecal microbial proteins and plasma free amino acids in normal men and ileostomates.

BACKGROUND: The importance of urea nitrogen reutilization in the amino acid economy of the host remains to be clarified. OBJECTIVE: The objective was to explore the transfer of (15)N from orally administered [(15)N(2)]urea or (15)NH(4)Cl to plasma free and intestinal microbial amino acids. DESIGN: Six men received an L-amino acid diet (167 mg N*kg(-)(1)*d(-)(1); 186 kJ*kg(-)(1)*d(-)(1)) for 11 d each on 2 different occasions. For the last 6 d they ingested [(15)N(2)]urea or, in random order, (15)NH(4)Cl (3.45 mg (15)N*kg(-)(1)*d(-)(1)). On day 10, a 24-h tracer protocol (12 h fasted/12 h fed) was conducted with subjects receiving the (15)N tracer hourly. In a similar experiment, (15)NH(4)Cl (3.9 mg (15)N*kg(-)(1)*d(-)(1)) was given to 7 ileostomates. (15)N Enrichments of urinary urea and plasma free and fecal or ileal microbial protein amino acids were analyzed. RESULTS: (15)N Retention was significantly higher with (15)NH(4)Cl (47.7%; P < 0.01) than with [(15)N(2)]urea (29.6%). Plasma dispensable amino acids after the (15)NH(4)Cl tracer were enriched up to 20 times (0. 2-0.6 (15)N atom% excess) that achieved with [(15)N(2)]urea. The (15)N-labeling pattern of plasma, ileal, and fecal microbial amino acids (0.05-0.45 (15)N atom% excess) was similar. Appearance of microbial threonine in plasma was similar for normal subjects (0.14) and ileostomates (0.17). CONCLUSION: The fate of (15)N from urea and NH(4)Cl differs in terms of endogenous amino acid metabolism, but is similar in relation to microbial protein metabolism. Microbial threonine of normal and ileostomy subjects appears in the blood plasma but the net contribution to the body threonine economy cannot be estimated reliably from the present data.

Adult↗
PubMed1999

Statistical analysis of nitrogen balance data with reference to the lysine requirement in adults.

Statistical analysis of nitrogen balance data is an important approach to the estimation of human nutrient requirement. The usual procedure is to regress nitrogen (N) balance on intake and to define the requirement as intake that would produce zero balance. In the actual application of this methodology, there are a number of options, and in the present study we explore the sensitivity of the regression approach to those options. To put this problem into a realistic context, we examine the current controversy over the lysine requirements of healthy adults. From early N balance studies, investigators concluded that the mean requirement was generally less than 10 mg. kg(-1). d(-1), whereas based on recent (13)C-tracer and metabolic studies, we propose a tentative mean requirement of approximately 30 mg. kg(-1). d(-1). Jones et al. (1956) conducted careful N balance studies from which they derived an estimate of lysine requirement of less than about 8 mg. kg(-1). d(-1). We reanalyzed these data with different choices of modes of analysis, mathematical models, and different assumptions concerning the magnitude of miscellaneous N losses. We find that for these data the choice of a specific mathematical model has only a small effect on resultant estimates of requirement, while estimated requirements are very sensitive to amount of unmeasured losses that are assumed and how the model is applied (whether the aggregate data are fitted in one pass to a single model, or the data for each individual subject are fitted to that individual's unique model). Moreover, our reanalysis suggests that the population requirement for lysine is in the range of 17 to 36 mg. kg(-1). d(-1) and strongly supports a lysine requirement value of about 30 mg. kg(-1). d(-1). In general, our results indicate that whenever possible, N balance data should be analyzed using a square root model fitted to individual data and that the median of the individual requirements so derived be used as the estimate of population requirement. Moreover, clearly any statistical analyses of N balance data should include a sensitivity analysis to determine the influence of underlying assumptions. Finally, the finding that these estimates are highly dependent on the assumed amount of N miscellaneous losses recommends that further studies on these losses and of the factors that influence them are essential.

Adult↗
PubMed1999

Plasma L-5-oxoproline carbon and nitrogen kinetics in healthy young adults.

L-5-oxoproline (OP), an intermediate of the gamma-glutamyl cycle of glutathione synthesis and degradation, may serve as a probe for the state of glutathione kinetics. We explored the whole-body carbon and nitrogen kinetics of OP in five male healthy subjects (75.2 kg; 181 cm; 26 y) after a 5-d adaptation to an adequate L-amino acid-based diet (160 mg N x kg(-1) x d(-1); 188 kJ x kg(-1) x d(-1)), using a crossover design. On day 6 of the diet period, we carried out an 8-h tracer protocol (3 h fast; 5 h fed; 2/3 of daily nitrogen intake) with intravenous infusion of L-[1-(13)C]oxoproline and L-[3, 3-(2)H]cysteine or, in randomized order, on the second occasion, L-[(15)N]oxoproline and L-[3,3-(2)H]cysteine. Plasma OP was isolated by cation exchange and after addition of internal standards (DL-[(2)H(3)]-5-oxoproline; L-[(15)N, U-(13)C(5)]-5-oxoproline; DL-[(2)H(3)]-glutamic acid) derivatized to form TBDMS esters and measured by gas chromatography/mass spectrometry. Plasma OP concentration did not differ between fed and fasted state (fast: 59. 4 +/- 8.3; fed 59.2 +/- 8.9 nmol/mL). (13)C- and (15)N OP flux during the fasted and fed state were 19 +/- 3.6, 21.2 +/- 3.2, and 22.6 +/- 3.9, 25.8 +/- 4.3 micromol x kg(-1) x 30 min(-1), respectively. OP oxidation was 15.6 +/- 3.6 and 17.9 +/- 3.5 micromol x kg(-1) x 30 min(-1), in fasting and feeding, respectively, (P < 0.05). More than 80% of the plasma flux was oxidized. These findings are compared with the published literature on GSH turnover in plasma of human subjects and underscore the need to define more completely the dynamic aspects of glutathione metabolism and of the intermediates of the gamma-glutamyl cycle.

Adult↗
PubMed1999

Adult human amino acid requirements.

This brief review is concerned with the status of our current understanding of the quantitative needs for dietary amino acids in healthy adults. The nutritional significance of the conditionally indispensable amino acids is assessed and the requirements for the indispensable amino acids are discussed. Recent research involving the use of the tracer balance approach is reviewed, and the importance of resolving the current uncertainties regarding adult human amino acid needs is highlighted.

Adult↗
PubMed1999

Effect of protein intake and physical activity on 24-h pattern and rate of macronutrient utilization.

Effects of moderate physical activity (90 min at 45-50% of maximal O2 uptake 2 times daily) and "high" (2.5 g protein. kg-1. day-1, n = 6) or "normal" protein intake (1.0 g protein. kg-1. day-1, n = 8) on the pattern and rate of 24-h macronutrient utilization in healthy adult men were compared after a diet-exercise-adjustment period of 6 days. Energy turnover (ET) was determined by indirect and direct (suit) calorimetry, and "protein oxidation" was determined by a 24-h continuous intravenous infusion of [1-13C]leucine. Subjects were in slight positive energy balance during both studies. Protein contributed to a higher (22 vs. 10%) and carbohydrate (CHO) a lower (33 vs. 58%) proportion of total 24-h ET on the high- vs. normal-protein intake. The highest contribution of fat to ET was seen postexercise during fasting (73 and 61% of ET for high and normal, respectively). With the high-protein diet the subjects were in a positive protein (P < 0.001) and CHO balance (P < 0.05) and a negative fat balance (P < 0.05). The increased ET postexercise was not explained by increased rates of urea production and/or protein synthesis.

Adolescent↗
PubMed1999

Availability of intestinal microbial lysine for whole body lysine homeostasis in human subjects.

We have investigated whether there is a net contribution of lysine synthesized de novo by the gastrointestinal microflora to lysine homeostasis in six adults. On two separate occasions an adequate diet was given for a total of 11 days, and a 24-h (12-h fast, 12-h fed) tracer protocol was performed on the last day, in which lysine turnover, oxidation, and splanchnic uptake were measured on the basis of intravenous and oral administration of L-[1-(13)C]lysine and L-[6,6-(2)H(2)]lysine, respectively. [(15)N(2)]urea or (15)NH(4)Cl was ingested daily over the last 6 days to label microbial protein. In addition, seven ileostomates were studied with (15)NH(4)Cl. [(15)N]lysine enrichment in fecal and ileal microbial protein, as precursor for microbial lysine absorption, and in plasma free lysine was measured by gas chromatography-combustion-isotope ratio mass spectrometry. Differences in plasma [(13)C]- and [(2)H(2)]lysine enrichments during the 12-h fed period were observed between the two (15)N tracer studies, although the reason is unclear, and possibly unrelated to the tracer form per se. In the normal adults, after (15)NH(4)Cl and [(15)N(2)]urea intake, respectively, lysine derived from fecal microbial protein accounted for 5 and 9% of the appearance rate of plasma lysine. With ileal microbial lysine enrichment, the contribution of microbial lysine to plasma lysine appearance was 44%. This amounts to a gross microbial lysine contribution to whole body plasma lysine turnover of between 11 and 130 mg. kg(-1). day(-1), depending on the [(15)N]lysine precursor used. However, insofar as microbial amino acid synthesis is accompanied by microbial breakdown of endogenous amino acids or their oxidation by intestinal tissues, this may not reflect a net increase in lysine absorption. Thus we cannot reliably estimate the quantitative contribution of microbial lysine to host lysine homeostasis with the present paradigm. However, the results confirm the significant presence of lysine of microbial origin in the plasma free lysine pool.

Adult↗
PubMed1998

Muscle protein synthesis by positron-emission tomography with L-[methyl-11C]methionine in adult humans.

Existing methods for assessing protein synthetic rates (PSRs) in human skeletal muscle are invasive and do not readily provide information about individual muscle groups. Recent studies in canine skeletal muscle yielded PSRs similar to results of simultaneous stable isotope measurements using L-[1-13C, methyl-2H3]methionine, suggesting that positron-emission tomography (PET) with L-[methyl-11C]methionine could be used along with blood sampling and a kinetic model to provide a less invasive, regional assessment of PSR. We have extended and refined this method in an investigation with healthy volunteers studied in the postabsorptive state. They received approximately 25 mCi of L-[methyl-11C]methionine with serial PET imaging of the thighs and arterial blood sampling for a period of 90 min. Tissue and metabolite-corrected arterial blood time activity curves were fitted to a three-compartment model. PSR (nmol methionine.min-1.g muscle tissue-1) was calculated from the fitted parameter values and the plasma methionine concentrations, assuming equal rates of protein synthesis and degradation. Pooled mean PSR for the anterior and posterior sites was 0.50 +/- 0.040. When converted to a fractional synthesis rate for mixed proteins in muscle, assuming a protein-bound methionine content of muscle tissue, the value of 0.125 +/- 0.01%.h-1 compares well with estimates from direct tracer incorporation studies, which generally range from approximately 0.05 to 0.09%.h-1. We conclude that PET can be used to estimate skeletal muscle PSR in healthy human subjects and that it holds promise for future in vivo, noninvasive studies of the influences of physiological factors, pharmacological manipulations, and disease states on this important component of muscle protein turnover and balance.

Adult↗
PubMed1998

A rabbit model for metabolic studies after burn injury.

BACKGROUND: A rabbit burn model was developed and characterized, which will allow conduct of repeated, noninvasive and more sophisticated in vivo metabolic studies to explore the pathophysiology of burn injury, owing to its larger blood volume and tissue mass than the rat. MATERIALS AND METHODS: A 20% body surface, full thickness burn was applied to the backs of six anesthetized rabbits by immersion into a boiling-water bath for 10 s, followed by resuscitation with saline. Resting energy expenditure (REE) was measured daily in pre- and postburn periods. Whole body protein kinetics were evaluated using L-[1(-13)C]leucine tracer, on the preburn and the third postburn day. Fasting plasma glucose was also measured. RESULTS: A significant elevation of REE began on the second postburn day and reached 34 +/- 8% above the preburn level (P < 0.05, paired t test) on the third postburn day. The fasting plasma leucine flux and oxidation were significantly elevated from their preburn levels (both P < 0.05), indicating an accelerated proteolysis and a more negative body protein balance (P < 0.05); however, the rate of whole body protein synthesis did not differ significantly pre- and postburn injury. Fasting plasma glucose also increased (P < 0.001). on the third postburn day. The burn scar remained intact during the study, without any sign of infection. CONCLUSIONS: The metabolic changes observed in this animal model can be attributed to burn injury per se and they mimic those for flow phase in burn patients. This rabbit burn model should be suitable for exploring mechanistic aspects of the burn-induced changes in metabolism and nutrient balance.

Animals↗
PubMed1998

Hyperglucagonemia and the immediate fate of dietary leucine: a kinetic study in humans.

The possible role of glucagon in determining the fate of dietary absorbed amino acids within the splanchnic bed was investigated in five healthy male volunteers. A kinetic study was performed involving a continuous 240-minute infusion of L-[5,5,5-2H3]leucine and D-[6,6-2H2]glucose by vein, while L-[1-13C]leucine was infused by a feeding tube into the duodenum (intragut [i.g.]) along with a constant intravenous (i.v.) infusion of somatotropin release-inhibitory factor (SRIF) combined with insulin, growth hormone, and glucagon. In random order, glucagon was infused at a rate of 0.4 ng x kg(-1) x min(-1) in one experiment and 1.2 ng x kg(-1) x min(-1) in the other experiment, while insulin and growth hormone were kept at constant serum levels, respectively, 37+/-13 pmol x L(-1) and 5+/-0.2 microg x L(-1). The diet was provided as an L-amino acid solution including 60 micromol x kg(-1) x h(-1) leucine without fat and carbohydrate. During the higher rate of glucagon infusion, there was an increase in plasma glucagon and glucose concentrations, glucose flux, and net dietary leucine release into the periphery from the splanchnic bed. Splanchnic removal and uptake of leucine were decreased with increased glucagon infusion. There were no statistical differences in the plasma leucine level and i.v. and i.g. leucine fluxes at the two glucagon levels, although leucine metabolic clearance increased (0.74 v 0.85 L x kg(-1) x h(-1), P=.08) in the case of glucagon excess. Plasma glucose increased with glucagon excess and was negatively correlated (P < .05) with the plasma leucine level (r=-.348) and i.v. (r=-.459) or i.g. (r=-.359) leucine fluxes. The negative correlation between plasma glucagon and leucine levels was also significant (r=-.684). No significant correlation was found between dietary leucine splanchnic removal and glucose, glucagon, or leucine plasma concentrations. We conclude that glucagon in excess has only a small quantitative effect on the overall handling of dietary leucine, and hypothesize that more leucine is exported to the peripheral tissues under these hormonal conditions.

Adult↗
PubMed1998

An initial assessment, using 24-h [13C]leucine kinetics, of the lysine requirement of healthy adult Indian subjects.

The international 1985 FAO/WHO/UNU upper dietary requirement for lysine of 12 mg.kg-1.d-1 may be inadequate for healthy Indian adults. To test this, we used a modified indicator amino acid oxidation technique to assess the adequacy of lysine intake of 12 and 28 mg.kg-1.d-1. Seven healthy, male, Indian subjects were studied during each of two randomly assigned 6-d periods while receiving an otherwise adequate diet based on an L-amino acid mixture. Beginning at 1800 on day 6 of the diet, a 24-h infusion protocol in which a [13C]leucine tracer was administered intravenously was used to assess leucine oxidation and daily leucine balance at each test lysine intake. Mean 24-h leucine oxidation was 54.7 compared with 46.9 mg.kg-1.d-1 (P < 0.05) and mean 24-h leucine balances were -4.1 and 3.5 mg.kg-1.d-1 (P < 0.05) for lysine intakes of 12 and 28 mg, respectively. Leucine balances were significantly negative (0.025 < P < 0.05) with the 12-mg lysine intake and not significantly different (P > 0.10) from zero or equilibrium with the 28-mg intake. These findings indicate that the international requirement for lysine appears to be inadequate to maintain body amino acid homeostasis and function in apparently healthy subjects characteristic of the south Asia region. They further indicate that our previously proposed, tentative lysine requirement of 30 mg.kg-1.d-1 is probably adequate for this population.

Adult↗
PubMed1998

Twenty-four-hour L-[1-(13)C]tyrosine and L-[3,3-(2)H2]phenylalanine oral tracer studies at generous, intermediate, and low phenylalanine intakes to estimate aromatic amino acid requirements in adults.

Daily pattern and rates of whole-body tyrosine oxidation and phenylalanine hydroxylation were determined in young adults (15 men, 1 woman) receiving [13C]tyrosine and [(2)H2]phenylalanine via primed, constant oral infusion and [(2)H4]tyrosine by vein (five subjects also received [(2)H3]leucine simultaneously by vein) continuously for 24 h (12 h fast then 12 h fed). Subjects were given a diet supplying 96.6 (n = 5), 35.6 (the proposed requirement; n = 5), and 18.5 mg phenylalanine x kg(-1) x d(-1) (n = 6) based on an otherwise adequate L-amino acid mixture for 6 d before the 24-h tracer study began. [Each diet was low in tyrosine: 6.79 mg x kg(-1) x d(-1).] Our hypothesis was that subjects would be in tyrosine equilibrium, positive balance, or both, at the 96.6- and 35.6-mg intakes and in distinctly negative balance at the 18.5-mg intake. The diurnal pattern in phenylalanine and tyrosine kinetics was dependent on the intake and, presumably, on the adequacy of dietary phenylalanine. Wholebody tyrosine balances, determined from rates of phenylalanine hydroxylation and tyrosine input and oxidation were negative (0.05 < P < 0.1 from zero balance) with the low (18.5 mg) phenylalanine intake [total aromatic amino acid (AAA) intake: 25.3 mg x kg(-1) x d(-1)] but at equilibrium (P > 0.05 from zero balance) with the two higher phenylalanine intakes. Whole-body AAA balance (AAA intake - tyrosine oxidation) was negative (P < 0.05 from zero balance) with the low intake, at equilibrium with the intermediate intake, and apparently distinctly positive (P < 0.05) with the generous intake. Despite model limitations, as discussed, these findings lend further support for a proposed, tentative value for a total mean requirement of 39 mg AAA x kg(-1) x d(-1).

Adolescent↗