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Biomedical subjects

Paul B Pencharz

Publications and source records attributed to Paul B Pencharz.

At least 19 recordsLinked to original sources

Coadministration of ornithine and alpha-ketoglutarate is no more effective than ornithine alone as an arginine precursor in piglets enterally fed an arginine-deficient diet.

Simultaneous administration of alpha-ketoglutarate and ornithine, in a 1:2 molar ratio, may improve the effectiveness of ornithine as an arginine precursor in neonatal piglets by shifting ornithine metabolism away from oxidation and toward the synthesis of arginine and other metabolically important compounds. To study this proposed mechanism, enterally fed piglets were allocated to receive 1 of 4 diets for 5 d: an arginine-deficient [1.2 mmol/(kg . d) arginine] diet (basal), or the basal diet supplemented with either alpha-ketoglutarate [4.6 mmol/(kg x d)] (+alpha-KG), ornithine [9.2 mmol/(kg x d)] (+Orn), or both ornithine and alpha-ketoglutarate (+alpha-KG/+Orn, molar ratio 1:2). Primed, constant infusions of [1-(14)C]ornithine given both intragastrically and intraportally were used to measure ornithine kinetics and determine the role of first-pass intestinal metabolism in ornithine metabolism. Whole body arginine and glutamate kinetics were measured using a primed, constant intragastric infusion of [guanido-(14)C]arginine and [3,4-(3)H]glutamate. The diets did not affect plasma arginine or ammonia concentrations, arginine flux, or arginine synthesis from ornithine. Therefore, arginine synthesis was not increased by the simultaneous infusion of ornithine and alpha-ketoglutarate. Piglets that received dietary ornithine had a 2-fold greater rate of proline synthesis from ornithine (P < 0.05) and oxidized a greater (P < 0.05) portion of the infused ornithine than piglets in the basal and +alpha-KG groups. Overall, ornithine addition to an arginine deficient diet had a greater effect on ornithine and arginine metabolism than the addition of alpha-ketoglutarate. First-pass intestinal metabolism was critical for ornithine synthesis and conversion to other metabolites but not for ornithine oxidation.

Administration, Oral↗

Effect of orthotopic liver transplantation (OLT) on branched-chain amino acid requirement.

Little is known regarding the impact of liver transplantation on amino acid requirements in children. Since plasma levels of the branched-chain amino acids (BCAA) are decreased in the presence of normal levels of the aromatic amino acids after liver transplantation, normalization of hepatic function may not fully correct changes in BCAA metabolism that occur in the pretransplant period. The goal of the present study was to determine total BCAA requirements of children following liver transplantation. The requirement of total BCAA was determined using indicator amino acid oxidation (IAAO) in five clinically stable children (5.7 +/- 3.5 y, mean +/- SD) 1-8 y post liver transplantation. Children received in random order 6 graded intakes of total BCAA. Individual BCAA in the test diet were provided in the same proportions as present in egg protein to minimize the potential interactive effects of individual BCAA on assessment of requirement. Total BCAA requirement was determined by measuring the oxidation of L-[1-13C] phenylalanine to 13CO2 [F13CO2 in micromol/kg/h], after a primed, continuous infusion of the tracer and using a two-phase linear regression crossover regression analysis. The estimated average requirement and the upper limit of the 95% CI for total BCAA in children who have undergone liver transplantation were 172 and 206 mg/kg/d), respectively. Total BCAA requirement in children who have undergone orthotopic liver transplantation (OLT) remain increased in the post-liver transplant period when compared with healthy school aged children, but is decreased when compared with children with mild-moderate chronic cholestatic (MCC) liver disease.

Amino Acids, Branched-Chain↗

Total sulfur amino acid requirement of healthy school-age children as determined by indicator amino acid oxidation technique.

BACKGROUND: Current total sulfur amino acid (TSAA) requirements of children are based on a factorial estimate that involves several assumptions. OBJECTIVE: The objective was to determine the TSAA requirement (methionine alone) of healthy school-age children by measuring the appearance of 13CO2 (F13CO2) in breath after the oxidation of l-[1-13C]phenylalanine in response to graded methionine intakes. DESIGN: Six healthy school-age children randomly received each of 6 methionine intakes (0, 5, 10, 15, 25, and 35 mg.kg(-1).d(-1)) along with an amino acid mixture to give a final protein intake of 1.5 g.kg(-1).d(-1) and an energy intake of 1.7 x resting energy expenditure. The diet was devoid of cysteine. The mean TSAA requirement was determined by applying a biphase linear regression crossover analysis on F13CO2 data, which identified a breakpoint at minimal F13CO2 in response to graded methionine intakes. RESULTS: The mean and population-safe (upper 95% CI) intakes of TSAA (as methionine) were determined to be 12.9 and 17.2 mg.kg(-1).d(-1), respectively. CONCLUSIONS: The current study suggests that children of this age group have a mean TSAA requirement similar to that of adults (12.6 mg.kg(-1).d(-1)). Therefore, it is valid to use a factorial approach, which assumes that maintenance requirements in childhood are similar to adult requirements, to estimate TSAA requirements in school-age children.

Amino Acids, Sulfur↗

Aromatic amino acid requirements in healthy men measured by indicator amino acid oxidation.

BACKGROUND: In the current literature, no agreement exists on estimates for aromatic amino acid (phenylalanine plus tyrosine) requirements as measured by stable-isotope techniques. OBJECTIVE: The goal of the present study was to determine the phenylalanine requirement in healthy men who were fed a diet without tyrosine by using the indicator amino acid oxidation method. DESIGN: Five healthy men were assigned to receive in random order diets devoid of tyrosine and with 8 graded intakes of phenylalanine (5, 10, 15, 25, 35, 45, 60, and 70 mg x kg(-1) x d(-1)). The phenylalanine requirement was measured by the rate of 13CO2 release (F13CO2) from L-[1-(13)C]lysine oxidation. RESULTS: The graded intakes of phenylalanine had no effect on lysine flux, as required for this method. The phenylalanine (ie, total aromatic amino acid) requirement, in the absence of tyrosine, was estimated to be 48 mg x kg(-1) x d(-1) by applying a two-phase linear regression crossover model to the F13CO2 data. CONCLUSIONS: In the absence of tyrosine, the mean phenylalanine requirement is higher than the current FAO/WHO/UNU (1985) and Dietary Reference Intake (2002) recommendations.

Adult↗

Minimum methionine requirement and cysteine sparing of methionine in healthy school-age children.

BACKGROUND: Cysteine can provide a portion of the sulfur amino acid requirement in adults. Whether this is true in children-and, if so, to what extent-is not known. OBJECTIVES: The objectives were to determine minimum methionine requirements in healthy, school-age children when excess cysteine is provided and to subsequently determine the cysteine-sparing effect by comparing these methionine requirements with those determined previously in the same children when no cysteine was provided. DESIGN: Six healthy, school-age children randomly received graded intakes of methionine (0, 2.5, 5, 7.5, 10, and 15 mg . kg(-1) . d(-1)) along with 21 mg cysteine . kg(-1) . d(-1) in the diet. The mean methionine requirement was determined by using a biphasic linear regression crossover analysis of measurements of the rate of appearance of (13)CO(2) in the breath (F(13)CO(2)), which identified a breakpoint at the minimal F(13)CO(2) in response to graded levels of methionine intake. RESULTS: The mean and population-safe minimum methionine requirements, in the presence of excess dietary cysteine, were found to be 5.8 and 7.3 mg . kg(-1) . d(-1), respectively. The mean and population-safe (upper 95% CI) methionine requirements, in the absence of dietary cysteine, were previously determined to be 12.9 and 17.2 mg . kg(-1) . d(-1), respectively. These values represent a cysteine-sparing effect of 55% and 58% in comparison with mean and population-safe methionine requirements, respectively. CONCLUSION: Excess intake of dietary cysteine results in the reduction in the requirements for methionine to a minimum obligatory requirement level.

Breath Tests↗

Branched-chain amino acid needs in children with mild-to-moderate chronic cholestatic liver disease.

Protein-energy malnutrition is prevalent in children with chronic cholestatic liver disease. Supplementation of branched-chain amino acids (BCAA) in infants and children with chronic liver disease has been associated with significant improvement in growth and nitrogen balance, suggesting that BCAA requirements are increased in chronic liver disease. The goal of the present study was to determine the total BCAA requirement in children with mild-to-moderate chronic cholestatic (MCC) liver disease using indicator amino acid oxidation (IAAO). Total BCAA requirements were determined in 6 children (6.3 +/- 3.7 y, mean +/- SD) with MCC liver disease. Children were randomly assigned to receive 7 graded intakes of total BCAA. Individual BCAA in the test diet were provided in the same proportions as those present in egg protein to minimize the potential interactive effects of individual BCAA on assessment of requirement. The total BCAA requirement was determined by measuring the oxidation of l-[1-13C] Phe to 13CO2 [F13CO2 in micromol/(kg x h)], after a primed, continuous oral administration of the tracer and using a 2-phase linear regression crossover regression analysis. The estimated mean requirement and the upper limit of the 95% CI for total BCAA establishing using the IAAO in children with MCC liver disease were 209 and 272 mg/(kg x d), respectively. Total BCAA estimated average requirements using the IAAO were significantly higher than mean requirements established previously for healthy children (P < 0.05).

Amino Acids, Branched-Chain↗

Leucine is not a good choice as an indicator amino acid for determining amino acid requirements in men.

Leucine tracer has been widely used for examining whole-body protein turnover in humans, but has not been evaluated as an indicator to be used in the indicator amino acid oxidation (IAAO) method. The goal of this study was to determine whether the L-[1-(13C)]leucine isotope is an acceptable indicator by comparing it with an established tracer, L-[1-(13C)]lysine. Healthy men (n = 7; 29.9 +/- 4.8 y old) were fed in random order a diet with 7 graded intakes of phenylalanine without tyrosine. In the first study (n = 5), subjects were administered an excess leucine intake of 65 mg/(kg.d), and in the second study (n = 5), they were given the mean requirement of 45 mg/(kg.d) to determine whether leucine intake affected the pattern of response. Previous IAAO studies using lysine and phenylalanine demonstrated a clear pattern in 13CO2 production, i.e., increasing test amino acid intake resulted in a linear decrease to plateau, with a readily discernable breakpoint indicating the requirement. This pattern of production of 13CO2, indicates clear partitioning of the indicator amino acid between oxidation and protein synthesis. This was not observed with leucine at an intake of 65 mg/(kg.d). Conversely, at the lower leucine intake of 45 mg/(kg.d), a breakpoint was seen and a total aromatic amino acid requirement estimate that did not differ from that obtain using lysine as the indicator was obtained. In conclusion, leucine may be used as the indicator in the IAAO technique only when the daily intake leucine is given at its mean requirement level and the potential metabolic effects of other variables are taken into consideration.

Adult↗

Mild-to-moderate chronic cholestatic liver disease increases leucine oxidation in children.

Malnutrition is prevalent in children with chronic cholestatic liver disease. Using the noninvasive indicator amino acid oxidation (IAAO) technique, we recently determined that mild-to-moderate chronic cholestatic (MCC) liver disease increases the need for branched-chain amino acids (BCAA) in children. To examine the underlying mechanisms responsible for this increased need for BCAA in liver disease, we measured L-[1-(13C)]-leucine oxidation in the postabsorptive and fed states in 10 children with MCC liver disease (8.8 +/- 3.5 y) and in 11 healthy children (9.4 +/- 2.2 y). The oxidation of L-[1-(13C)]-leucine to 13CO2 [F13CO2 in micromol/(kg.h)] was determined after a primed, continuous oral administration of the tracer. Total BCAA in diet was provided at 300 mg/(kg.d) to ensure that leucine oxidation was measured when leucine intake was in excess of requirements. In the postabsorptive state, the rate of release of 13CO2 from 13C-leucine oxidation (F13CO2) and whole-body leucine oxidation were significantly higher in children with MCC liver disease (P < 0.05). However, F13CO2 and whole-body leucine oxidation did not differ in the fed state. We conclude that the increased need for dietary BCAA in MCC liver disease is mediated in part by increased leucine oxidation in the postabsorptive state.

Amino Acids, Branched-Chain↗

The in vivo sparing of methionine by cysteine in sulfur amino acid requirements in animal models and adult humans.

Sulfur amino acid metabolism has been receiving increased attention because of the link to chronic diseases such as cardiovascular disease, Alzheimer's disease, and diabetes. In addition, the role of cysteine and optimal intakes for physiological substrates such as glutathione are currently of considerable interest in human health. Although the dietary indispensability of methionine is not in question, the ability of cysteine to substitute for a portion of its requirement has been the topic of much debate. Methionine is often the most limiting amino acid in the diets of the developing world's population because of its low concentration in cereal grains. Therefore, the ability of cysteine to substitute for methionine requirement is not just biologically interesting; it is also of considerable economic and social importance. The primary goal of this review is to discuss the available evidence on the effect of cysteine substitution for methionine to meet the total sulfur amino acid requirement in adult humans, including an assessment of the methodological features of experiments with conflicting results. Assessment of the requirement experiments for amino acids with complex metabolism such as methionine and cysteine must begin with a careful definition of requirements and what substitution means. As a result of these definitions, a set of criteria for the intakes of methionine that will allow demonstration of the substitution effect have been developed. Some recent publications are assessed using these definitions and criteria, and a possible reason for the conflicting results in the literature is proposed. An approach to estimating tolerable upper intakes is also proposed. Research on in vivo sulfur amino acid metabolism in humans is tremendously difficult, and therefore, we do not wish to be overly critical of the high-quality work of the ambitious and highly intelligent men and women who have conducted various studies. Our goal is to objectively review the data for the reader in a logical and comprehensive manner and propose methods that may avoid difficulties in future studies.

Amino Acids, Sulfur↗

Citrulline is an effective arginine precursor in enterally fed neonatal piglets.

Although neonatal piglets can synthesize some arginine from proline, there is a limit to this synthesis, and piglets fed an arginine-deficient diet have diminished whole-body arginine status. To help elucidate where the limitation in arginine synthesis may occur, our objective was to determine the most effective arginine precursor in 1-wk-old enterally fed piglets. Piglets were administered either an arginine-deficient (basal) diet [1.15 mmol arginine/(kg.d)] or the basal diet supplemented with equimolar [9.18 mmol/(kg.d)] amounts of proline (+Pro), ornithine (+Orn), citrulline (+Cit) or arginine (+Arg) for 5 d (n = 5/diet). Daily blood samples were taken and indicators of whole-body arginine status including plasma amino acid, ammonia, and urea concentrations were measured. A primed, constant intragastric (i.g.) infusion of l-[U-(14)C]proline was given to measure the proline to arginine conversion, and intravenous (i.v.) and i.g. infusions of l-[guanido-(14)C]arginine were given to determine arginine flux and to quantify the splanchnic extraction of dietary arginine. Piglets fed the +Cit and +Arg diets had lower plasma ammonia and urea concentrations (P < 0.05) and higher plasma arginine concentrations (P < 0.0001) and arginine fluxes (P < 0.05) than piglets fed the other 3 diets. Piglets fed +Cit and +Arg had a lower proline to arginine conversion (P < 0.05). During first-pass splanchnic metabolism, 52% of the dietary arginine was extracted, and this extraction was not affected by whole-body arginine status (P > 0.05). These data indicate that citrulline, but not ornithine or proline, is an effective arginine precursor, and that either citrulline formation or availability appears to limit arginine synthesis in neonatal piglets.

Amino Acids↗

L-rhamnose and lactulose decrease serum triacylglycerols and their rates of synthesis, but do not affect serum cholesterol concentrations in men.

Colonic short-chain fatty acids (SCFA) may affect hepatic lipid metabolism. Lactulose increases colonic acetate production, whereas L-rhamnose increases propionate. To test the effects of oral L-rhamnose and lactulose for 28 d on fasting concentrations and hepatic synthesis of lipids in humans, 18 men were administered 25 g/d of L-rhamnose, lactulose, or d-glucose for 4 wk in a partially randomized crossover design, with blood collected from fasting subjects on the first and last day of each period. Cholesterol and triacylglycerol (TG) synthesis rates were determined using deuterated water uptake rate over the last 24 h of each period. Postprandial blood lipids, and glucose and insulin were assessed in 11 subjects on d 28. Fasting serum cholesterol was unchanged; however, when expressed as a percentage change, TG were decreased, relative to baseline (P < 0.04), by L-rhamnose (-10%) and lactulose (-10%), compared with D-glucose, which increased serum TG (+11%). Net TG-fatty acid (TGFA) synthesis on d 28 was lower with L-rhamnose (2.42 +/- 0.38 g/d) and lactulose (2.62 +/- 0.35 g/d) than with D-glucose (2.96 +/- 0.31 g/d, P < 0.01). We conclude that these results do not support a primary role for propionate in the cholesterol-lowering effect of soluble fiber. However, both lactulose and L-rhamnose lowered serum TG (expressed as a percentage change) and TGFA synthesis, compared with d-glucose, which increased them. Although these data are consistent with inhibition of TGFA synthesis by SCFA, other aspects of the metabolism of these sugars cannot be ruled out as putative agents of their TG-lowering effects.

Adult↗

Enteric-coated pancreatic enzyme with bicarbonate is equal to standard enteric-coated enzyme in treating malabsorption in cystic fibrosis.

OBJECTIVES: To compare the efficacy of an enteric-coated buffered pancreatic enzyme (EC buffered PE) containing 1.5 mEq of bicarbonate per capsule with a conventional enteric-coated enzyme (EC-PE) capsule in cystic fibrosis patients with signs or symptoms of moderate to severe malabsorption. METHODS: In a double-blind crossover study, subjects were randomly assigned to two consecutive, 2-week phases using an EC buffered PE product and conventional EC-PE product. Seventy-two hour stool collections from each phase were analyzed for energy, fat, and nitrogen content and expressed as percent of estimated intake. RESULTS: Twenty-one patients with cystic fibrosis and pancreatic insufficiency (14 female, mean age 20.6 +/- 11.5 years, range 8.8-41.9) completed the study. There was no significant difference in percent malabsorption of energy (19.4% vs. 19.0%), fat (20.7% vs. 20.2%), or nitrogen (10.4% vs. 10.7%) between the EC buffered PE product and the conventional EC-PE product. However, patients taking the EC buffered PE product received less enzyme based on actual enzyme activity measured in vitro (3,468 +/- 1,434 U lipase/g fat vs. 3,978 +/- 1,474 U lipase/g fat, P < 0.02). CONCLUSIONS: In the doses used, nutrient absorption of patients taking EC buffered PE preparation offers no advantage over a conventional EC-PE preparation.

Adolescent↗

Amino acid requirements of infants and children.

Nitrogen balances have been conducted in preterm infants, preschool children, and 6- to 10-year-old children to determine dietary indispensable amino acid. A recent review concluded that the data, being sufficiently uncertain, could not be used as the basis for defining amino acid requirements in infants and children. Therefore, it was decided to use a factorial approach (basal plus growth). This approach is based on the assumption that basal requirements are the same throughout the life cycle. Recently, using indicator oxidation, the requirements of the eight classical indispensable amino acids have been defined in adults. These values have been used as the basal component of requirement in childhood. The growth component was based on the changes in body protein with age. We have recently shown that the maintenance requirements for branched chain amino acids are similar in children and adults, thereby validating the factorial approach.

Age Factors↗

Arginine synthesis does not occur during first-pass hepatic metabolism in the neonatal piglet.

We have shown that first-pass intestinal metabolism is necessary for approximately 50% of whole body arginine synthesis from its major precursor proline in neonatal piglets. Furthermore, the intestine is not the site of increased arginine synthesis observed during dietary arginine deficiency. Primed constant intravenous (iv) and intraportal (ip) infusions of L-[U-14C]proline, and iv infusion of either L-[guanido-14C]arginine or L-[4,5-3H]arginine were used to measure first-pass hepatic arginine synthesis in piglets enterally fed either deficient (0.20 g.kg(-1).day(-1)) or generous (1.80 g.kg(-1).day(-1)) quantities of arginine for 5 days. Conversion of arginine to other urea cycle intermediates and arginine recycling were also calculated for both dietary treatments. Arginine synthesis (g.kg(-1).day(-1)) from proline was greater in piglets (P < 0.05) fed the deficient arginine diet in both the presence (generous: 0.07; deficient: 0.17; pooled SE = 0.01) and absence (generous: 0.06; deficient: 0.20; pooled SE = 0.01) of first-pass hepatic metabolism. There was no net arginine synthesis from proline during first-pass hepatic metabolism regardless of arginine intake. Arginine conversion to urea, citrulline, and ornithine was significantly greater (P < 0.05) in piglets fed the generous arginine diet. Calculated arginine fluxes were significantly lower (P = 0.01) for [4,5-3H]arginine than for [guanido-14C]arginine, and the discrepancy between the values was greater in piglets fed the deficient arginine diet (35% vs. 20%). Collectively, these findings show that first-pass hepatic metabolism is not a site of net arginine synthesis and that piglets conserve dietary arginine in times of deficiency by decreasing hydrolysis and increasing recycling.

Amino Acids↗

Combining unprotected pancreatic enzymes with pH-sensitive enteric-coated microspheres does not improve nutrient digestion in patients with cystic fibrosis.

OBJECTIVES: To assess the efficacy of combining unprotected powder enzymes and oral enteric-coated microsphere (ECM) and to ECM alone in treating nutrient maldigestion in patients with cystic fibrosis. STUDY DESIGN: Patients were randomly assigned into 2 consecutive, 2-week phases; ECM alone, and ECM plus unprotected powder enzymes. Fecal fat, energy, and nitrogen output were compared with intake at the end of each phase. Two-tailed, paired t tests were performed to compare outcomes. RESULTS: The mean age of the 14 patients (3 girls) was 5.7 +/- 3.2 years (range, 1.9 to 13.4 years). There was no significant difference in percent malabsorption of fat (15.6% vs 18.2%), energy (13.3% vs 13.4%), or nitrogen (11.8% vs 11.3%) between phases. CONCLUSIONS: The addition of powder enzymes to ECM did not improve nutrient maldigestion compared with ECM alone.

Adolescent↗

Changes in response to insulin and the effects of varying glucose tolerance on whole-body protein metabolism in patients with cystic fibrosis.

BACKGROUND: Diabetes mellitus has been reported to increase whole-body protein breakdown and thus loss of lean body mass. Cystic fibrosis-related diabetes (CFRD) is associated with undernutrition and increased mortality. OBJECTIVE: We hypothesized that CFRD is associated with increased whole-body protein breakdown, which results in negative protein balance, and that correction of the glucose intolerance with insulin therapy would normalize whole-body protein metabolism. DESIGN: Rates of whole-body protein turnover and protein balance were measured in 28 adults with cystic fibrosis (17 M, 11 F). Subjects were assessed with a modified oral-glucose-tolerance test and categorized as having normal glucose tolerance, impaired glucose tolerance, or CFRD with and without fasting hyperglycemia; then they were compared with previously diagnosed CFRD adults already receiving insulin therapy. Indexes of protein turnover were calculated from [15N]glycine and 15N in urinary urea. RESULTS: Analysis of variance for the 28 subjects showed that whole-body protein breakdown was highest (P<0.05) in patients with CFRD. Whole-body protein synthesis was not significantly affected by impaired glucose tolerance. Significant (P<0.05) improvement in net protein synthesis occurred in the CFRD group 3 mo after insulin therapy was administered. Follow-up studies of 3 subjects with CFRD showed significant improvement in net protein synthesis after insulin therapy. Monitoring of the protein homeostasis of the impaired glucose tolerance group gave clues to the progression of their metabolic homeostasis. CONCLUSION: CFRD has an adverse effect on protein homeostasis by increasing net protein synthesis.

Adult↗

Development of the indicator amino acid oxidation technique to determine the availability of amino acids from dietary protein in pigs.

Standardized ileal ("true") digestibility is currently the best estimate of amino acid digestibility, but it does not measure bioavailability. Growth assays to determine amino acid bioavailability are expensive and laborious; thus, a rapid method is needed. Applying the principle of slope-ratio assay to the indicator amino acid oxidation (IAAO) method, we hypothesized that the reduction in indicator oxidation per gram of lysine in feedstuffs relative to that per gram of free lysine represented the bioavailability of lysine, here termed "metabolic availability." Indicator oxidation in pigs was linear over increasing lysine intakes (r = 0.90, P = 0.001) when the dietary lysine contents were 2 SD below the mean lysine requirement of the pigs. Peas were treated (raw, heated to reduce lysine availability, or heated with added lysine) to test the responsiveness of the IAAO to differing lysine availability. Free lysine reduced indicator oxidation by 3.16% of dose oxidized per gram added lysine, whereas the addition of protein lysine as raw (-2.81%) and heated peas (-1.73%) reduced oxidation to a lesser degree. Adding free lysine to heated peas decreased indicator oxidation, evidence that heating had worsened the utilization of pea protein for protein synthesis by reducing the bioavailability of lysine alone. Pea diets differed only in the availability of lysine; therefore IAAO detected differences in lysine bioavailability. Because the IAAO technique responds to lysine available at the sites of protein synthesis, the metabolic availability covers all losses during digestion, absorption, and utilization of lysine. This method can determine the metabolic availability of amino acids of a feedstuff within 2 wk.

Amino Acids↗