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10 Protein and Amino Acids SUMMARY Protein is the major structural component of all cells in the body. Proteins also function as enzymes, in membranes, as transport carriers, and as hormones; and their component amino acids serve as precursors for nucleic acids, hormones, vitamins, and other important molecules. The Recommended Dietary Allowance (RDA) for both men and women is 0.80 g of good quality protein/kg body weight/d and is based on careful analyses of available nitrogen balance studies. For amino acids, isotopic tracer methods and linear regression analysis were used whenever possible to deter- mine the requirements. The estimated average requirements for amino acids were used to develop amino acid scoring patterns for various age groups based on the recommended intake of dietary protein. The recommended protein digestibility corrected amino acid scoring pattern (PDCAAS) for proteins for children 1 year of age and older and all other age groups is as follows (in mg/g of protein): isoleucine, 25; leucine, 55; lysine, 51, methionine + cysteine (SAA), 25; phenylalanine + tyrosine, 47; threonine, 27; tryptophan, 7; valine, 32; and histidine, 18. While an upper range for total protein in the diet as a percent of total energy intake was set at no more than 35 percent to decrease risk of chronic disease (see Chapter 11), there were insufficient data to provide dose–response relationships to establish a Tolerable Upper Intake Level (UL) for total protein or for any of the amino acids. However, the absence of a UL means that caution is warranted in using any single amino acid at levels significantly above that normally found in food. 589

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590 DIETARY REFERENCE INTAKES BACKGROUND INFORMATION Chemistry of Proteins and Amino Acids Protein Protein is the major functional and structural component of all the cells of the body; for example, all enzymes, membrane carriers, blood transport molecules, the intracellular matrices, hair, fingernails, serum albumin, keratin, and collagen are proteins, as are many hormones and a large part of membranes. Moreover, the constituent amino acids of protein act as precursors of many coenzymes, hormones, nucleic acids, and other molecules essential for life. Thus an adequate supply of dietary protein is essential to maintain cellular integrity and function, and for health and reproduction. Proteins in both the diet and body are more complex and variable than the other energy sources, carbohydrates and fats. The defining char- acteristic of protein is its requisite amino (or imino) nitrogen group. The average content of nitrogen in dietary protein is about 16 percent by weight, so nitrogen metabolism is often considered to be synonymous with protein metabolism. Carbon, oxygen, and hydrogen are also abundant elements in proteins, and there is a smaller proportion of sulfur. Proteins are macromolecules consisting of long chains of amino acid subunits. The structures for the common L-amino acids found in typical dietary proteins are shown in Figure 10-1. In the protein molecule, the amino acids are joined together by peptide bonds, which result from the elimination of water between the carboxyl group of one amino acid and the α-amino (or imino in the case of proline) group of the next in line. In biological systems, the chains formed might be anything from a few amino acid units (di, tri, or oligopeptide) to thousands of units long (polypeptide), corresponding to molecular weights ranging from hundreds to hundreds of thousands of Daltons. The sequence of amino acids in the chain is known as the primary structure. A critical feature of proteins is the complexity of their physical struc- tures. Polypeptide chains do not exist as long straight chains, nor do they curl up into random shapes, but instead fold into a definite three- dimensional structure. The chains of amino acids tend to coil into helices (secondary structure) due to hydrogen bonding between side chain residues, and sections of the helices may fold on each other due to hydrophobic interactions between nonpolar side chains and, in some proteins, to disulfide bonds so that the overall molecule might be globular or rod-like (tertiary structure). Their exact shape depends on their function and for some proteins, their interaction with other molecules (quaternary structure).

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591 P ROTEIN AND AMINO ACIDS Name Abbreviation Form Aliphatic side chains H CH COOH Glycine Gly NH2 CH3 CH COOH A lanine Ala NH2 Valine a CH3 Val CH CH COOH CH3 NH2 a CH3 Leucine Leu CH CH2 CH COOH CH3 NH2 a CH3 CH2 Isoleucine Ile CH CH COOH CH3 NH2 Aromatic side chains Phenylalanine Phe CH2 CH COOH NH2 Tyrosine Tyr HO CH2 CH COOH NH2 Tryptophan Trp CH2 CH COOH NH2 N H Hydroxyl groups in side chains CH2 CH COOH Serine Ser OH NH2 CH2 CH CH COOH Threonine Thr OH NH2 Sulfur-containing side chains Cysteine b HS CH2 CH COOH Cys NH2 CH3 S CH2 CH2 CH COOH Methionine Met NH2 Imino Acids CH2 CH3 c Pro Proline CH COOH CH2 N H Acidic side chains and their amides HOOC CH2 CH2 CH COOH Glutam Glu NH2 O Glutamine Gln H2N C CH2 CH2 CH COOH NH2 HOOC CH2 CH COOH Aspartic acid Asp NH2 O Asparagione Asn H2N C CH2 CH COOH NH2 Basic side chains H2N CH2 CH2 CH2 CH2 CH COOH Lysine Lys NH2 H Arginine Arg H2N C N CH2 CH2 CH2 CH COOH NH NH2 CH2 CH COOH Histidine His N NH NH2 A mino acids in italics are classed as nutritionally indispensable to humans. a Leucine, valine, and isoleucine are known as the branched-chain amino acids. b Cysteine is often found as a dimer (cysteine), linked through sulfur atoms (-S-S-) by oxidation. c Proline is, strictly speaking, an imino acid rather than an amino acid. FIGURE 10-1 L-amino acids of nutritional significance.

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592 DIETARY REFERENCE INTAKES Many proteins are composed of several separate peptide chains held together by ionic or covalent links, an example being hemoglobin, in which each active unit consists of two pairs of dissimilar subunits (the α and β chains). The most important aspect of a protein from a nutritional point of view is its amino acid composition, but the protein’s structure may also influ- ence its digestibility. Some proteins, such as keratin, are highly insoluble in water and hence are resistant to digestion, while highly glycosylated proteins, such as the intestinal mucins, are resistant to attack by the proteolytic enzymes of the intestine. Amino Acids The amino acids that are incorporated into mammalian protein are α-amino acids, with the exception of proline, which is an α-imino acid. This means that they have a carboxyl group, an amino nitrogen group, and a side chain attached to a central α-carbon (Figure 10-1). Functional differences among the amino acids lie in the structure of their side chains. In addition to differences in size, these side groups carry different charges at physiological pH (e.g., nonpolar, uncharged but polar, negatively charged, positively charged); some groups are hydrophobic (e.g., branched chain and aromatic amino acids) and some hydrophilic (most others). These side chains have an important bearing on the ways in which the higher orders of protein structure are stabilized and are intimate parts of many other aspects of protein function. Attractions between positive and negative charges pull different parts of the molecule together. Hydrophobic groups tend to cluster together in the center of globular proteins, while hydrophilic groups remain in contact with water on the periphery. The ease with which the sulfhydryl group in cysteine forms a disulfide bond with the sulfhydryl group of another cysteine in a polypeptide chain is an important factor in the stabilization of folded structures within the poly- peptide and is a crucial element in the formation of inter-polypeptide bonds. The hydroxyl and amide groups of amino acids provide the sites for the attachment of the complex oligosaccharide side chains that are a feature of many mammalian proteins such as lactase, sucrase, and the mucins. Histidine and amino acids with the carboxyl side chains (glutamic acid and aspartic acid) are critical features in ion-binding proteins, such as the calcium-binding proteins (e.g., troponin C), critical for muscular con- traction, and the iron-binding proteins (e.g., hemoglobin) responsible for oxygen transport. Some amino acids in protein only achieve their final structure after their precursors have been incorporated into the polypeptide. Notable examples of such post-translational modifications are the hydroxyproline

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593 P ROTEIN AND AMINO ACIDS and hydroxylysine residues found in collagen (proline and lysine are con- verted to these after they have been incorporated into procollagen) and 3-methylhistidine present in actin and myosin. The former hydroxylated amino acids are critical parts of the cross-linking of collagen chains that lead to rigid and stable structures. The role of methylated histidine in contractile protein function is unknown. Nutritional and Metabolic Classification of Amino Acids Older views of the nutritional classification of amino acids categorized them into two groups: indispensable (essential) and dispensable (non- essential). The nine indispensable amino acids (Table 10-1) are those that have carbon skeletons that cannot be synthesized to meet body needs from simpler molecules in animals, and therefore must be provided in the diet. Although the classification of the indispensable amino acids and their assignment into a single category has been maintained in this report, the definition of dispensable amino acids has become blurred as more infor- mation on the intermediary metabolism and nutritional characteristics of these compounds has accumulated. Laidlaw and Kopple (1987) divided dispensable amino acids into two classes: truly dispensable and condition- ally indispensable. Five of the amino acids in Table 10-1 are termed dis- pensable as they can be synthesized in the body from either other amino TABLE 10-1 Indispensable, Dispensable, and Conditionally Indispensable Amino Acids in the Human Diet Conditionally Precursors of Conditionally Indispensable a Indispensable Dispensable Indispensable Histidineb Alanine Arginine Glutamine/glutamate, asparate Isoleucine Aspartic acid Cysteine Methionine, serine Leucine Asparagine Glutamine Gl utamic acid/ammonia Lysine Glutamic acid Glycine Serine, choline Methionine Serine Proline Glutamate Phenylalanine Tyrosine Phenylalanine Threonine Tryptophan Valine a Conditionally indispensable is defined as requiring a dietary source when endogenous synthesis cannot meet metabolic need. b Although histidine is considered indispensable, unlike the other eight indispensable amino acids, it does not fulfill the criteria used in this report of reducing protein deposition and inducing negative nitrogen balance promptly upon removal from the diet. SOURCE: Laidlaw and Kopple (1987).

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594 DIETARY REFERENCE INTAKES acids or other complex nitrogenous metabolites. In addition, six other amino acids, including cysteine and tyrosine, are conditionally indispens- able as they are synthesized from other amino acids or their synthesis is limited under special pathophysiological conditions (Chipponi et al., 1982; Harper, 1983; Laidlaw and Kopple, 1987). This is even more of an issue in the neonate where it has been suggested that only alanine, aspartate, glutamate, serine, and probably asparagine are truly dietarily dispensable (Pencharz et al., 1996). The term conditionally indispensable recognizes the fact that under most normal conditions the body can synthesize these amino acids to meet metabolic needs. However, there may be certain physiological circum- stances: prematurity in the young infant where there is an inadequate rate at which cysteine can be produced from methionine; the newborn, where enzymes that are involved in quite complex synthetic pathways may be present in inadequate amounts as in the case of arginine (Brunton et al., 1999), which results in a dietary requirement for this amino acid; or patho- logical states, such as severe catabolic stress in an adult, where the limited tissue capacity to produce glutamine to meet increased needs and to bal- ance increased catabolic rates makes a dietary source of these amino acids required to achieve body nitrogen homeostasis. The cells of the small intestine become important sites of conditionally indispensable amino acid, synthesis, with some amino acids (e.g., glutamine and arginine) becoming nutritionally indispensable under circumstances of intestinal metabolic dysfunction (Stechmiller et al., 1997). However, the quantita- tive requirement levels for conditionally indispensable amino acids have not been determined and these, presumably, vary greatly according to the specific condition. There now appears to be a requirement for preformed α-amino nitrogen in the form of glutamate, alanine, or aspartate, for example (Katagiri and Nakamura, 2002). It was previously thought that, in addition to the indispensable amino acids, simple sources of nitrogen such as urea and diammonium citrate together with carbon sources would be sufficient to maintain nitrogen homeostasis (FAO/WHO, 1965). However, there are now good theoretical reasons to conclude that this is not likely in the human (Katagiri and Nakamura, 2002). The mixture of dispensable and conditionally indispensable amino acids as supplied by food proteins at adequate intakes of total nitrogen will assure that both the nitrogen and specific amino acid needs are met.

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595 P ROTEIN AND AMINO ACIDS Protein and Amino Acid Homeostasis Maintenance of Body Protein Body Protein Reserve. The body of a 70-kg man contains about 11 kg of protein. Nearly half of this protein (about 43 percent) is present as skeletal muscle, while other structural tissues such as skin and blood each contain approximately 15 percent of the total protein (Lentner, 1981). The meta- bolically active visceral tissues (e.g., liver and kidney) contain compara- tively small amounts of protein (together about 10 percent of the total). Other organs such as the brain, lung, heart, and bone contribute the remainder. The distribution among the organs varies with developmental age, as the newborn infant has proportionately less muscle and much more brain and visceral tissue than the adult. It is also notable that, despite the very wide variety of enzymes and proteins within a single organism, almost one half of the total protein content of the human is present in just four proteins (myosin, actin, collagen, and hemoglobin). Collagen in particular may comprise 25 percent of the total. Moreover, in induced malnutrition, this proportion can rise to 50 percent because of the substantial loss of noncollagen proteins, whereas collagen itself is retained (Picou et al., 1966). Even in the adult, when the protein mass of the body has reached a plateau, it can be influenced by a variety of nutritional and pathological factors. Thus, when diets high or low in protein are given, there is a gain or loss of body protein over the first few days, before re-equilibration of protein intake with the rates of oxidation and excretion (Swick and Benevenga, 1977). This phenomenon has led to the concept of a “labile protein reserve,” which can be gained or lost from the body as a short-term store for use in emergencies or to take account of day-to-day variations in dietary intake. Studies in animals have suggested that this immediate labile protein store is contained in the liver and visceral tissues, as their protein content decreases very rapidly during starvation or protein depletion (by as much as 40 percent), while skeletal muscle protein drops much more slowly (Swick and Benevenga, 1977). During this situation, protein break- down becomes a source of indispensable amino acid needs for synthesis of proteins critical to maintaining essential body function (Reeds et al., 1994). This labile protein reserve in humans is unlikely to account for more than about 1 percent of total body protein (Waterlow, 1969; Young et al., 1968). Thus, the immediately accessible stores of protein (which serve as the source of indispensable amino acids and amino nitrogen) cannot be considered in the same light as the huge energy stores in the form of body fat; the labile protein reserve is similar in weight to the glycogen store. However, it should be recognized that this protein reserve is unlike the fat

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596 DIETARY REFERENCE INTAKES and glycogen stores, whose primary roles are for energy use. The protein lost during fasting is functional body protein and thus there is no evidence for a protein reserve that serves only as a store to meet future needs. There is a wide range of variation in daily dietary protein intake, from the protein requirement and beyond, to which the body is able to adapt over a period of days, after which no further change in body protein con- tent occurs. However, pathological conditions, such as severe disease states, can cause substantial rates of protein loss due to the increased demand for either amino acids or carbon skeletons to meet local energy demands. If these conditions go unchecked for more than a few days, there may be a serious depletion of the body’s protein mass, which might eventually become life threatening. Although the evidence from short-term changes in diet suggests that the main loss of protein is from the viscera (de Blaauw et al., 1996), in chronic illness skeletal muscle, which comprises over 40 percent of the protein mass of a healthy individual, becomes the largest single contributor to protein loss (Hansen et al., 2000). Free Amino Acids. Although the free amino acids dissolved in the body fluids are only a very small proportion of the body’s total mass of amino acids, they are very important for the nutritional and metabolic control of the body’s proteins. The content of free and protein-bound amino acids in rat muscle is shown in Table 10-2. It can be seen that their ranges are considerable and that their concentrations in the free pool are in no way related to their concentrations in body proteins. In the human, free phenylalanine com- prises less than 2 percent of its total body pool, and corresponds to only about 1.5 hour worth of protein synthesis, or 25 percent of the day’s intake of protein (Waterlow et al., 1978). Free glutamate and alanine comprise a larger proportion of their respective body pools, but they could not be considered as reserves for more than a very short time. In human muscle, glutamine has an exceptionally large free pool, containing about 10 to 15 g of nitrogen. After trauma, this pool can become depleted by more than 50 percent (Labow and Souba, 2000); its loss may then make a significant contribution to the total loss of nitrogen. Although the plasma compartment is most easily sampled, the concen- tration of most amino acids is higher in tissue intracellular pools. Typically, large neutral amino acids, such as leucine and phenylalanine, are essen- tially in equilibrium with the plasma. Others, notably glutamine, glutamic acid, and glycine, are 10- to 50-fold more concentrated in the intracellular pool. Dietary variations or pathological conditions can result in substantial changes in the concentrations of the individual free amino acids in both the plasma and tissue pools (Furst, 1989; Waterlow et al., 1978).

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597 P ROTEIN AND AMINO ACIDS TABLE 10-2 Comparison of the Pool Sizes of Free and Protein-Bound Amino Acids in Rat Muscle µmol/g Wet Weight Protein: Free Protein Free Ratio Indispensable amino acids Histidine 26 0.39 67 Isoleucine 50 0.16 306 Leucine 109 0.20 556 Lysine 58 1.86 31 Methionine 36 0.16 225 Phenylalanine 45 0.07 646 Threonine 60 1.94 31 Valine 83 0.31 272 Dispensable and some conditionally indispensable amino acids Alanine 111 2.77 40 Arginine 67 0.25 269 Aspartic acid (+ amide) 110 1.13 97 Glutamic acid (+ amide) 148 9.91 15 Glycine 117 1.94 60 Serine 74 1.96 38 Tyrosine 36 0.14 266 SOURCE: Data of E.B. Fern, quoted by Waterlow et al. (1978). Pathways of Amino Acid Metabolism The exchange between body protein and the free amino acid pool is illustrated by the highly simplified scheme shown in Figure 10-2. Here, all the proteins in the tissues and circulation are grouped into one pool. Similarly, there is a second pool, consisting of the free amino acids dis- solved in body fluids. The arrows into and out of the protein pool show the continual degradation and resynthesis of these macromolecules (i.e., pro- tein turnover). The other major pathways that involve the free amino acid pool are the supply of amino acids by the gut from the absorbed amino acids derived from dietary proteins, the de novo synthesis in cells (includ- ing those of the gut, which are a source of dispensable amino acids), and the loss of amino acids by oxidation, excretion, or conversion to other metabolites. Although this scheme represents protein metabolism in the human as a whole, with minor modifications it can also be used to repre-

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598 DIETARY REFERENCE INTAKES De Novo Synthesis Dietary Intake (dispensable) Protein Turnover Degradation Tissue Free Amino Acids Protein Synthesis Protein Losses Skin Non-Protein Excretion Hair Pathways Feces Oxidation FIGURE 10-2 Exchange between body protein and free amino acid pools. sent protein metabolism in individual organs, or indeed the metabolism of a single protein. Amino Acid Utilization for Growth Dietary protein is not only needed for maintaining protein turnover and the synthesis of physiologically important products of amino acid metabolism but is, of course, laid down as new tissue. Studies in animals show that the composition of amino acids needed for growth is very simi- lar to the composition of body protein (Dewey et al., 1996). It is important to note, however, that the amino acid composition of human milk is not the same as that of body protein (Dewey et al., 1996), and although the present recommendations for the dietary amino acids for infants provided in this report continue to be based on human milk as the standard, recent authors (Dewey et al., 1996) have cautioned that the composition of human milk proteins is not necessarily a definition of the biological amino acid requirements of the growing neonate. Maintenance Protein Needs Even when mammals consume no protein, nitrogen continues to be lost. Provided that the energy intake is adequate, these “basal” losses are closely related to body weight and basal metabolic rate (Castaneda et al., 1995b; Scrimshaw et al., 1972). In man, normal growth is very slow and the dietary requirement to support growth is small in relation to maintenance needs except at very young ages. Moreover, the human being is a long-

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599 P ROTEIN AND AMINO ACIDS lived species. It follows that maintenance needs are of particular impor- tance to humans and account for a very large majority of lifetime needs for dietary protein. It has been known for decades (Said and Hegsted, 1970) that the body’s capacity to conserve individual amino acids at low intakes varies, so the pattern of amino acids needed in the diet to match their individual catabolic rates does not correspond precisely with the composition of body protein. For example, the indispensable amino acid requirements for adults may provide a quarter of their minimum total need for amino nitrogen, compared with the need for noncollagen body protein in which approxi- mately half of the amino acids are indispensable (FAO/WHO/UNU, 1985). This implies that there is very effective recycling of indispensable amino acids released continuously from protein degradation back into protein synthesis. Under conditions where the diet is devoid of protein, the efficiency of amino acid recycling is over 90 percent for both indis- pensable and dispensable amino acids (Neale and Waterlow, 1974). While highly efficient, some amino acids are recycled at different rates than others. Physiology of Absorption, Metabolism, and Excretion Protein Digestion and Absorption After ingestion, proteins are denatured by the acid in the stomach, where they are also cleaved into smaller peptides by the enzyme pepsin, which is activated by the increase in stomach acidity that occurs on feed- ing. The proteins and peptides then pass into the small intestine, where the peptide bonds are hydrolyzed by a variety of enzymes. These bond- specific enzymes originate in the pancreas and include trypsin, chymotrypsins, elastase, and carboxypeptidases. The resultant mixture of free amino acids and small peptides is then transported into the mucosal cells by a number of carrier systems for specific amino acids and for di- and tri-peptides, each specific for a limited range of peptide substrates. After intracellular hydrolysis of the absorbed peptides, the free amino acids are then secreted into the portal blood by other specific carrier systems in the mucosal cell or are further metabolized within the cell itself. Absorbed amino acids pass into the liver, where a portion of the amino acids are taken up and used; the remainder pass through into the systemic circulation and are utilized by the peripheral tissues. Although there are good reasons to suppose that dietary protein diges- tion is incomplete and variable among different diets, recent studies using proteins intrinsically labeled with 15N added to a diet suggest that many common dietary proteins, including proteins from casein, mixed whey, wheat, and legumes, are digested with an efficiency of greater than 90 per-

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758 DIETARY REFERENCE INTAKES Nommsen LA, Lovelady CA, Heinig MJ, Lönnerdal B, Dewey KG. 1991. Determi- nants of energy, protein, lipid, and lactose concentrations in human milk during the first 12 mo of lactation: The DARLING Study. Am J Clin Nutr 53:457–465. Oddoye EA, Margen S. 1979. Nitrogen balance studies in humans: Long-term effect of high nitrogen intake on nitrogen accretion. J Nutr 109:363–377. Ohmura E, Aoyama Y, Yoshida A. 1986. Changes in lipids in liver and serum of rats fed a histidine-excess diet or cholesterol-supplemented diets. Lipids 21:748–753. Oishi R, Furuno K, Gomita Y, Araki Y, Saeki K. 1989. Effect of acute treatment of mice with L-histidine on the brain levels of amino acids. J pn J Pharmacol 49:143–146. Olivo M, Kitahama K, Valatx JL, Jouvet M. 1986. Neonatal monosodium glutamate dosing alters the sleep-wake cycle of the mature rat. Neurosci Lett 67:186–190. Olney JW. 1969. Brain lesions, obesity, and other disturbances in mice treated with monosodium glutamate. Science 164:719–721. Olney JW. 1989. Glutamate, a neurotoxic transmitter. J Child Neurol 4:218–226. Olney JW. 1994. Excitotoxins in foods. Neuro Toxicol 15:535–544. Olney JW, Ho OL. 1970. Brain damage in infant mice following oral intake of glutamate, aspartate or cysteine. Nature 227:609–611. Olney JW, Cicero TJ, Meyer ER, de Gubareff T. 1976. Acute glutamate-induced eleva- tions in serum testosterone and luteinizing hormone. Brain Res 112:420–424. Owen G, Cherry CP, Prentice DE, Worden AN. 1978a. The feeding of diets contain- ing up to 4% monosodium glutamate to rats for 2 years. Toxicol Lett 1:221–226. Owen G, Cherry CP, Prentice DE, Worden AN. 1978b. The feeding of diets con- taining up to 10% monosodium glutamate to beagle dogs for 2 years. Toxicol Lett 1:217–219. Park KG, Heys SD, Blessing K, Kelly P, McNurlan MA, Eremin O, Garlick PJ. 1992. Stimulation of human breast cancers by dietary L-arginine. Clin Sci 82:413–417. Patrick J, Pencharz PB, Belmonte M, Ste-Marie M, Boland MP, Issenman RM, Van Aerde JEE, Rousseau-Harsany E. 1994. Undernutrition in children with neuro- developmental disability. Can Med Assoc J 151:753–759. Pellett PL, Young VR. 1992. The effects of different levels of energy intake on protein metabolism and of different levels of protein intake on energy metabolism: A statistical evaluation from the published literature. In: Scrimshaw NS, Schürch B, eds. Protein-Energy Interaction. Lausanne, Switzerland: IDECG, Nestlé Foun- dation. Pp. 81–121. Pencharz PB. 1985. Body composition and growth. In: Walker A, ed. Nutrition in Pediatrics. Basic Science and Clinical Application. Boston. Little, Brown. Pp. 77–85. Pencharz PB, Azcue M. 1996. Use of bioelectrical impedance analysis (BIA) measurements in the clinical management of malnutrition. Am J Clin Nutr 64:S485–S488. Pencharz BP, House JD, Wykes LJ, Ball RO. 1996. What are the essential amino acids for the preterm and term infant? In: Bindels JG, Goedhart A, Visser HKA, eds. R ecent Developments in Infant Nutrition. Nutricia Symposia Vol. 9. Dordrecht, The Netherlands: Kluwer Academic Publishers. Pp. 278–296. Pepplinkhuizen L, Bruinvels J, Blom W, Moleman P. 1980. Schizophrenia-like psy- chosis caused by a metabolic disorder. Lancet 1:454–456. Perry TL, Hardwick DF, Dixon GH, Dolman CL, Hansen S. 1965. Hyper- methioninemia: A metabolic disorder associated with cirrhosis, islet cell hyperplasia, and renal tubular degeneration. Pediatrics 36:236–250. Persaud TV. 1969. The foetal toxicity of leucine in the rat. West Indian Med J 18:34–39.

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