Below are the first 10 and last 10 pages of uncorrected machine-read text (when available) of this chapter, followed by the top 30 algorithmically extracted key phrases from the chapter as a whole.
Intended to provide our own search engines and external engines with highly rich, chapter-representative searchable text on the opening pages of each chapter. Because it is UNCORRECTED material, please consider the following text as a useful but insufficient proxy for the authoritative book pages.
Do not use for reproduction, copying, pasting, or reading; exclusively for search engines.
OCR for page 589
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
OCR for page 590
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).
OCR for page 591
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.
OCR for page 592
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
OCR for page 593
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).
OCR for page 594
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.
OCR for page 595
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
OCR for page 596
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).
OCR for page 597
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-
OCR for page 598
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-
OCR for page 599
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-
OCR for page 758
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.
OCR for page 759
759 P ROTEIN AND AMINO ACIDS Peters JC, Harper AE. 1987. Acute effects of dietary protein on food intake, tissue amino acids, and brain serotonin. Am J Physiol 252:R902–R914. Picou D, Halliday D, Garrow JS. 1966. Total body protein, collagen and non- collagen protein in infantile protein malnutrition. Clin Sci 30:345–351. Pilc A, Rogoz Z, Skuza G. 1982. Histidine-induced bizarre behaviour in rats: The possible involvement of central cholinergic system. Neuropharmacology 21:781–785. Pinals RS, Harris ED, Burnett JB, Gerber DA. 1977. Treatment of rheumatoid arthritis with L-histidine: A randomized, placebo-controlled, double-blind trial. J Rheumatol 4:414–419. Pineda O, Torun B, Viteri FE, Arroyave G. 1981. Protein quality in relation to estimates of essential amino acids requirements. In: Bodwell CE, Adkins JS, Hopkins DT, eds. Protein Quality in Humans: Assessment and In Vitro Estimation. Westport, CT: AVI Publishing. Pp. 29–42. Pinto-Scognamiglio W, Amorico L, Gatti GL. 1972. Toxicity and tolerance to mono- sodium glutamate studied by a conditioned avoidance test. Farmaco 27:19–27. Pipe NGJ, Smith T, Halliday D, Edmonds CJ, Williams C, Coltart TM. 1979. Changes in fat, fat-free mass and body water in human normal pregnancy. Br J Obstet Gynaecol 86:929–940. Pizzi WJ, Barnhart JE, Fanslow DJ. 1977. Monosodium glutamate administration to the newborn reduces reproductive ability in female and male mice. Science 196:452–454. Pizzi WJ, Tabor JM, Barnhart JE. 1978. Somatic, behavioral, and reproductive dis- turbances in mice following neonatal administration of sodium L-aspartate. Pharmacol Biochem Behav 9:481–485. Pollitt E. 2000. Developmental sequel from early nutritional deficiencies: Conclu- sive and probability judgements. J Nutr 130:350S–353S. Poon TK, Cameron DP. 1978. Measurement of oxygen consumption and locomotor activity in monosodium glutamate-induced obesity. Am J Physiol 234:E532–E534. Porter PB, Griffin AC. 1950. Effects of glutamic acid on maze learning and recovery from electroconvulsive shocks in albino rats. J Comp Physiol Psychol 43:1–15. Pradhan SN, Lynch JF. 1972. Behavioral changes in adult rats treated with mono- sodium glutamate in the neonatal stage. Arch Int Pharmacodyn Ther 197:301–304. Pratt EL, Snyderman SE, Cheung MW, Norton P, Holt LE. 1955. The threonine requirement of the normal infant. J Nutr 56:231–251. Prentice AM, Goldberg GR, Prentice A. 1994. Body mass index and lactation per- formance. Eur J Clin Nutr 48:S78–S86. Prosky L, O’Dell RG. 1972. Biochemical changes of brain and liver in neonatal offspring of rats fed monosodium-L-glutamate. Experientia 28:260–263. Raguso CA, Pereira P, Young VR. 1999. A tracer investigation of obligatory oxida- tive amino acids losses in healthy, young adults. Am J Clin Nutr 70:474–483. Räihä N, Minoli I, Moro G. 1986a. Milk protein intake in the term infant I: Meta- bolic responses and effects on growth. Acta Paediatr Scand 75:881–886. Räihä N, Minoli I, Moro G. 1986b. Milk protein intake in the term infant II: Effects on plasma amino acid concentrations. Acta Paediatr Scand 75:887–892. Raiten DJ, Talbot JM, Fisher KD. 1995. Analysis of Adverse Reactions to Monosodium Glutamate (MSG). Bethesda, MD: Federation of American Societies for Experi- mental Biology. Ramsey BW, Farrell P, Pencharz PB. 1992. Nutritional assessment and manage- ment in cystic fibrosis: a consensus report. Am J Clin Nutr 55:108–116.
OCR for page 760
760 DIETARY REFERENCE INTAKES Rand WM, Young VR. 1999. Statistical analysis of nitrogen balance data with refer- ence to the lysine requirement in adults. J Nutr 129:1920–1926. Rand WM, Young VR, Scrimshaw NS. 1976. Change of urinary nitrogen excretion in response to low-protein diets in adults. Am J Clin Nutr 29:639–644. Rand WM, Scrimshaw NS, Young VR. 1981. Conventional (“long-term”) nitrogen balance studies for protein quality evaluation in adults: Rationale and limita- tions. In: Bodwell CE, Adkins JS, Hopkins DT, eds. Protein Quality in Humans: Assessment and In Vitro Estimation. Westport, CT: AVI Publishing. Pp. 61–94. Rand RM, Pellett PL, Young VR. 2003. Meta-analysis of nitrogen balance studies for estimating protein requirements in healthy adults. Am J Clin Nutr 77:109–127. Reeds PJ, Burrin DG. 2001. Glutamine and the bowel. J Nutr 131:2505S–2508S. Reeds PJ, Garlick PJ. 1984. Nutrition and protein turnover in man. Adv Nutr Res 6:93–138. Reeds PJ, Field CR, Jahoor F. 1994. Do the differences between the amino acid compositions of acute-phase and muscle proteins have a bearing on nitrogen loss in traumatic states? J Nutr 124:906–910. Reif-Lehrer L. 1976. Possible significance of adverse reactions to glutamate in humans. Fed Proc 35:2205–2211. Rennie MJ, Edwards RH, Krywawych S, Davies CT, Halliday D, Waterlow JC, Millward DJ. 1981. Effect of exercise on protein turnover in man. Clin Sci (Lond) 61:627–639. Reynolds JV, Thom AK, Zhang SM, Ziegler MM, Naji A, Daly JM. 1988. Arginine, protein malnutrition, and cancer. J Surg Res 45:513–522. Reynolds JV, Daly JM, Shou J, Sigal R, Ziegler MM, Naji A. 1990. Immunologic effects of arginine supplementation in tumor-bearing and non-tumor-bearing hosts. Ann Surg 211:202–210. Reynolds JV, O’Farrelly C, Feighery C, Murchan P, Leonard N, Fulton G, O’Morain C, Keane FB, Tanner WA. 1996. Impaired gut barrier function in malnour- ished patients. Br J Surg 83:1288–1291. Reynolds MS, Steel DL, Jones EM, Baumann CA. 1958. Nitrogen balances of women maintained on various levels of methionine and cystine. J Nutr 64:99–111. Reynolds WA, Stegink LD, Filer LJ Jr, Renn E. 1980. Aspartame administration to the infant monkey: Hypothalamic morphology and plasma amino acid levels. Anat Rec 198:73–85. Rich LF, Beard ME, Burns RP. 1973. Excess dietary tyrosine and corneal lesions. Exp Eye Res 17:87–97. Rigo J, Senterre H. 1980. Optimal threonine intake for preterm infants fed on oral or parenteral nutrition. J Parenteral Enteral Nutr 4:15–17. Roberton AM, Rabel B, Harding CA, Tasman-Jones C, Harris PJ, Lee SP. 1991. Use of the ileal conduit as a model for studying human small intestinal mucus glycoprotein secretion. Am J Physiol 261:G728–G734. Roberts S. 1996. Energy requirements of older individuals. Eur J Clin Nutr 50:S112– S118. Roberts S, Thorpe JM, Ball RO, Pencharz PB. 2001. Tyrosine requirement of healthy men receiving a fixed phenylalanine intake determined by using indi- cator amino acid oxidation. Am J Clin Nutr 73:276–282. Rodwell VW. 1990. Conversion of amino acids to specialized products. In: Murray RK, Mayes PA, Granner DK, Rodwell VW, eds. Harper’s Biochemistry, 22nd ed. Norwalk, CT: Appleton & Lange. Pp. 307–313. Rogan WJ, Gladen BC. 1993. Breast-feeding and cognitive development. Early Human Dev 31:181–193.
OCR for page 761
761 P ROTEIN AND AMINO ACIDS Roig JC, Meetze WH, Auestad N, Jasionowski T, Veerman M, McMurray CA, Neu J. 1996. Enteral glutamine supplementation for the very low birthweight infant: Plasma amino acid concentrations. J Nutr 126:1115S–1120S. Ronnenberg AG, Gross KL, Hartman WJ, Meydani SN, Prior RL. 1991. Dietary arginine supplementation does not enhance lymphocyte proliferation or interleukin-2 production in young and aged rats. J Nutr 121:1270–1278. Rose DP, Leklem JE, Fardal L, Baron RB, Shrago E. 1977. Effect of oral alanine loads on the serum triglycerides of oral contraceptive users and normal subjects. Am J Clin Nutr 30:691–694. Rose WC. 1957. The amino acid requirements of adult man. Nutr Abs Rev 27:631–647. Rose WC, Haines WJ, Warner DT, Johnson JE. 1951. The amino acid requirements of man. II. The role of threonine and histidine. J Biol Chem 188:49–58. Rose WC, Borman A, Coon MJ, Lambert GF. 1955a. The amino acid requirements of man. X. The lysine requirement. J Biol Chem 214:579–587. Rose WC, Coon MJ, Lambert GF. 1955b. The amino acid requirements of man. VIII. The metabolic availability of the optical isomers of acetyltryptophan. J Biol Chem 212:201–205. Rose WC, Coon MJ, Lockhart HB, Lambert GF. 1955c. The amino acid require- ments of man. XI. The threonine and methionine requirements. J Biol Chem 215:101–110. Rose WC, Eades CH, Coon MJ. 1955d. The amino acid requirements of man. XII. The leucine and isoleucine requirements. J Biol Chem 216:225–234. Rose WC, Leach BE, Coon MJ, Lambert GF. 1955e. The amino acid requirements of man. IX. The phenylalanine requirement. J Biol Chem 213:913–922. Rose WC, Wixom RL, Lockhart HB, Lambert GF. 1955f. The amino acid require- ments of man. XV. The valine requirement; Summary and final observations. J Biol Chem 217:987–995. Rosenberg LE, Downing S, Durant JL, Segal S. 1966. Cystinuria: Biochemical evi- dence for three genetically distinct diseases. J Clin Invest 45:365–371. Rudman D, DiFulco TJ, Galambos JT, Smith RB, Salam AA, Warren WD. 1973. Maximal rates of excretion and synthesis of urea in normal and cirrhotic sub- jects. J Clin Invest 52:2241–2249. Ryan-Harshman M, Leiter LA, Anderson GH. 1987. Phenylalanine and aspartame fail to alter feeding behavior, mood and arousal in men. Physiol Behav 39:247–253. Said AK, Hegsted DM. 1970. Response of adult rats to low dietary levels of essential amino acids. J Nutr 100:1362–1375. Sauberlich HE. 1961. Studies on the toxicity and antagonism of amino acids for weanling rats. J Nutr 75:61–72. Schaafsma G. 2000. The protein digestibility-corrected amino acid score. J Nutr 130:1865S–1867S. Schainker B, Olney JW. 1974. Glutamate-type hypothalamic-pituitary syndrome in mice treated with aspartate or cysteate in infancy. J Neural Trans 35:207–215. Schaumburg HH, Byck R. 1968. Sin cib-syn: Accent on glutamate. N Engl J Med 279:105. Schaumburg HH, Byck R, Gerstl R, Mashman JH. 1969. Monosodium L-glutamate: Its pharmacology and role in the Chinese restaurant syndrome. S cience 163:826–828. Schechter PJ, Prakash NJ. 1979. Failure of oral L-histidine to influence appetite or affect zinc metabolism in man: A double-blind study. A m J Clin Nutr 32:1011–1014.
OCR for page 762
762 DIETARY REFERENCE INTAKES Scholl TO, Hediger ML, Ances IG. 1990. Maternal growth during pregnancy and decreased infant birth weight. Am J Clin Nutr 51:790–793. Scholl TO, Hediger ML, Schall JI, Khoo C-S, Fischer RL. 1994. Maternal growth during pregnancy and the competition for nutrients. Am J Clin Nutr 60:183–188. Schwartz JC, Lampart C, Rose C. 1972. Histamine formation in rat brain in vivo: Effects of histidine loads. J Neurochem 19:801–810. Schwartzstein RM, Kelleher M, Weinberger SE, Weiss JW, Drazen JM. 1987. Airways effects of monosodium glutamate in subjects with chronic stable asthma. J Asthma 24:167–172. Scrimshaw NS, Hussein MA, Murray E, Rand WM, Young VR. 1972. Protein require- ments of man: Variations in obligatory urinary and fecal nitrogen losses in young men. J Nutr 102:1595–1604. Scriver CR, Kaufman S, Woo SL. 1989. The hyperphenylalaninemias. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The Metabolic Basis of Inherited Disease, 6th ed. New York: McGraw-Hill. Pp. 495–546. Semprini ME, Frasca MA, Mariani A. 1971. Effects of monosodium glutamate (MSG) administration on rats during the intrauterine life and the neonatal period. Quaderni delle Nutrizione 31:85–100. Sen Gupta J, Srivastava KK. 1973. Effect of potassium-magnesium aspartate on endurance work in man. Ind J Exp Biol 11:392–394. Shaw GM, Velie EM, Schaffer DM. 1997. Is dietary intake of methionine associated with a reduction in risk for neural tube defect-affected pregnancies? Teratology 56:295–299. Simon CA, Van Melle GD, Ramelet AA. 1985. Failure of lysine in frequently recur- rent herpes simplex infection. Arch Dermatol 121:167–168. Simon RA. 2000. Additive-induced urticaria: Experience with monosodium glutamate (MSG). J Nutr 130:1063S–1066S. Sivam SP, Chermak T. 1992. Neonatal administration of L-cysteine does not pro- duce long-term effects on neurotransmitter or neuropeptide systems in the rat striatum. Res Comm Chem Pathol Pharm 77:219–225. Skeie B, Kvetan V, Gil KM, Rothkopf MM, Newsholme EA, Askanazi J. 1990. Branch-chain amino acids: Their metabolism and clinical utility. Crit Care Med 18:549–571. Smith B, Prockop DJ. 1962. Central-nervous-system effects of ingestion of L- tryptophan by normal subjects. N Engl J Med 267:1338–1341. Snyderman SE, Pratt EL, Cheung MW, Norton P, Holt LE, Hansen AE, Panos TC. 1955. The phenylalanine requirement of the normal infant. J Nutr 56: 253–263. Snyderman SE, Holt LE, Smellie F, Boyer A, Westall RG. 1959a. The essential amino acid requirements of infants: Valine. Am J Dis Child 97:186–191. Snyderman SE, Norton PM, Fowler DI, Holt LE. 1959b. The essential amino acid requirements of infants: Lysine. Am J Dis Child 97:175–185. Snyderman SE, Boyer A, Phansalkar SV, Holt LE. 1961a. Essential amino acid requirements of infants. Tryptophan. Am J Dis Child 102:41–45. Snyderman SE, Roitman EL, Boyer A, Holt LE. 1961b. Essential amino acid require- ments of infants. Leucine. Am J Dis Child 102:35–40. Snyderman SE, Boyer A, Roitman E, Holt LE, Prose PH. 1963. The histidine requirement of the infant. Pediatrics 31:786–801. Snyderman SE, Boyer A, Norton PM, Roitman E, Holt LE. 1964a. The essential amino acid requirements of infants. IX. Isoleucine. Am J Clin Nutr 15:313–321.
OCR for page 763
763 P ROTEIN AND AMINO ACIDS Snyderman SE, Boyer A, Norton PM, Roitman E, Holt LE. 1964b. The essential amino acid requirements of infants. X. Methionine. Am J Clin Nutr 15:322–330. Sole MJ, Benedict CR, Myers MG, Leenen FH, Anderson GH. 1985. Chronic dietary tyrosine supplements do not affect mild essential hypertension. Hypertension 7:593–596. Solomon JK, Geison RL. 1978. Effect of excess dietary L-histidine on plasma cholesterol levels in weanling rats. J Nutr 108:936–943. Souba WW. 1993. Glutamine and cancer. Ann Surg 218:715–728. Speth JD. 1989. Early hominid hunting and scavenging: The role of meat as an energy source. J Hum Evol 18:329–343. Speth JD, Spielmann KA. 1983. Energy source, protein metabolism, and hunter- gatherer subsistence strategies. J Anthropol Archaeol 2:1–31. Stechmiller JK, Treloar D, Allen N. 1997. Gut dysfunction in critically ill patients: A review of the literature. Am J Crit Care 6:204–209. Steele RD, Barber TA, Lalich J, Benevenga NJ. 1979. Effects of dietary 3- methylthiopropionate on metabolism, growth and hematopoiesis in the rat. J Nutr 109:1739–1751. Stefansson V. 1944a. Arctic Manual. New York: Macmillan. Stefansson V. 1944b. Pemmican. Military Surg 95:89–98. Stegink LD. 1976. Absorption, utilization, and safety of aspartic acid. J Toxicol Environ Health 2:215–242. Stegink LD, Shepherd JA, Brummel MC, Murray LM. 1974. Toxicity of protein hydrolysate solutions: Correlation of glutamate dose and neuronal necrosis to plasma amino acid levels in young mice. Toxicology 2:285–299. Stegink LD, Filer LJ, Baker GL. 1977. Effect of aspartame and aspartate loading upon plasma and erythrocyte free amino acid levels in normal adult volun- teers. J Nutr 107:1837–1845. Stegink LD, Filer LJ, Baker GL. 1980. Plasma methionine levels in normal adult subjects after oral loading with L-methionine and N-acetyl-L-methionine. J Nutr 110:42–49. Stegink LD, Filer LJ, Baker GL. 1982a. Plasma and erythrocyte amino acid levels in normal adult subjects fed a high protein meal with and without added mono- sodium glutamate. J Nutr 112:1953–1960. Stegink LD, Filer LJ, Baker GL. 1982b. Plasma and urinary methionine levels in one-year-old infants after oral loading with L-methionine and N-acetyl-L- methionine. J Nutr 112:597–603. Stegink LD, Filer LJ Jr, Baker GL. 1983a. Effect of carbohydrate on plasma and erythrocyte glutamate levels in humans ingesting large doses of monosodium L-glutamate in water. Am J Clin Nutr 37:961–968. Stegink LD, Filer LJ Jr, Baker GL. 1983b. Plasma amino acid concentrations in normal adults fed meals with added monosodium L-glutamate and aspartame. J Nutr 113:1851–1860. Stekol JA, Szaran J. 1962. Pathological effects of excessive methionine in the diet of growing rats. J Nutr 77:81–90. Stellar E, McElroy WD. 1948. Does glutamic acid have any effect on learning? Science 108:281–283. Stephenson LS, Lathan MC, Ottesen EA. 2000. Global malnutrition. Parasitology 121:S5–S22. Stevenson DD. 2000. Monosodium glutamate and asthma. J Nutr 130:1067S–1073S.
OCR for page 764
764 DIETARY REFERENCE INTAKES Stokes AF, Belger A, Banich MT, Taylor H. 1991. Effects of acute aspartame and acute alcohol ingestion upon the cognitive performance of pilots. Aviat Space Environ Med 62:648–653. Stoll B, Henry J, Reeds PJ, Yu H, Jahoor F, Burrin DG. 1998. Catabolism dominates the first-pass intestinal metabolism of dietary essential amino acids in milk protein-fed piglets. J Nutr 128:606–614. Strain GW, Strain JJ, Zumoff B. 1985. L-Tryptophan does not increase weight loss in carbohydrate-craving obese subjects. Int J Obes 9:375–380. Sweetman L. 1989. Branched chain organic acidurias. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The Metabolic Basis of Inherited Disease, 6th ed. New York: McGraw-Hill. Pp. 791–819. Swick RW, Benevenga NJ. 1977. Labile protein reserves and protein turnover. J Dairy Sci 60:505–515. Tachibana K Mukai K, Hiraoka I, Moriguchi S, Takama S, Kishino Y. 1985. Evalua- tion of the effect of arginine-enriched amino acid solution on tumor growth. J Parenter Enteral Nutr 9:428–434. Tarasoff L, Kelly MF. 1993. Monosodium L-glutamate: A double-blind study and review. Food Chem Toxicol 31:1019–1035. Tarnopolsky MA, MacDougall JD, Atkinson SA. 1988. Influence of protein intake and training status on nitrogen balance and lean body mass. J Appl Physiol 64:187–193. Tarnopolsky MA, Atkinson SA, MacDougall JD, Senor BB, Lemon PW, Schwarcz H. 1991. Whole body leucine metabolism during and after resistance exercise in fed humans. Med Sci Sports Exerc 23:326–333. Taverner MR, Hume ID, Farrell DJ. 1981. Availability to pigs of amino acids in cereal grains. 1. Endogenous levels of amino acids in ileal digesta and faeces of pigs given cereal diets. Br J Nutr 46:149–158. Terry LC, Epelbaum J, Martin JB. 1981. Monosodium glutamate: Acute and chronic effects on rhythmic growth hormone and prolactin secretion, and somatostatin in the undisturbed male rat. Brain Res 217:129–142. Thein DJ, Hurt WC. 1984. Lysine as a prophylactic agent in the treatment of recur- rent herpes simplex labialis. Oral Surg 58:659–666. Thoemke F, Huether G. 1984. Breeding rats on amino acid imbalanced diets for three consecutive generations affects the concentrations of putative amino acid transmitters in the developing brain. Int J Dev Neurosci 2:567–574. Thompson GN, Halliday D. 1992. Protein turnover in pregnancy. Eur J Clin Nutr 46:411–417. Torun B, Viteri FE. 1981. Obligatory nitrogen losses and factorial calculations of protein requirements of pre-school children. In: Torun B, Young VR, Rand WM, eds. Protein-Energy Requirements of Developing Countries: Evaluation of New Data. Tokyo, Japan: United Nations University Press. Pp. 159–163. Torun B, Cabrera Santiago M, Viteri FE. 1981. Protein requirements of pre-school children: Milk and soybean protein isolate. In: Torun B, Young VR, Rand WM, eds. Protein-Energy Requirements of Developing Countries: Evaluation of New Data. Tokyo, Japan: United Nations University Press. Pp. 182–190. Uauy R, Scrimshaw NS, Young VR. 1978. Human protein requirements: Nitrogen balance response to graded levels of egg protein in elderly men and women. Am J Clin Nutr 31:779–785.
OCR for page 765
765 P ROTEIN AND AMINO ACIDS Uauy R, Yanez E, Ballester D, Barrera G, Guzman E, Saitua MT, Zacaris I. 1981. Obligatory urinary and faecal nitrogen losses in young Chilean men fed two levels of dietary energy intake. In: Torun B, Young VR, Rand WM, eds. Protein- Energy Requirements of Developing Countries: Evaluation of New Data. Tokyo, Japan: United Nations University Press. van Acker BA, von Meyenfeldt MF, van der Hulst RR, Hulsewe KW, Wagenmakers AJ, Deutz NE, de Blaauw I, Dejong CH, van Kreel BK, Soeters PB. 1999. Glutamine: The pivot of our nitrogen economy? J P arenter Enteral Nutr 23:S45–S48. van der Schoor SRD, van Goudoever JB, Stoll B, Henry JF, Rosenberger JR, Burrin DG, Reeds PJ. 2001. The pattern of intestinal substrate oxidation is altered by protein restriction in pigs. Gastroenterology 121:1167–1175. van Raaij JMA, Pee MEM, Vermaat-Miedema SH, Schonk CM, Hautvast JGAJ 1988. New equations for estimating body fat mass in pregnancy from body density or total body water. Am J Clin Nutr 48:24–29. van Wouwe JP, Hoogenkamp S, Van den Hamer CJ. 1989. Histidine supplement and Zn status in Swiss random mice. Biol Trace Elem Res 22:35–43. Viau AT, Leathem JH. 1973. Excess dietary methionine and pregnancy in the rat. J Reprod Fertil 33:109–111. Vijayasarathy C, Khan-Siddiqui L, Murthy SN, Bamji MS. 1987. Rise in plasma trimethyllysine levels in humans after oral lysine load. A m J Clin Nutr 46:772–777. Villalpando S, Butte NF, Flores-Huerta S, Thotathuchery M. 1998. Qualitative analysis of human milk produced by women consuming a maize-predominant diet typical of rural Mexico. Ann Nutr Metab 42:23–32. Viteri FE, Martinez C. 1981. Integumental nitrogen losses of pre-school children with different levels and sources of dietary protein intake. In: Torun B, Young VR, Rand WM, eds. Protein-Energy Requirements of Developing Countries: Evalua- tion of New Data. Tokyo, Japan: United Nations University Press. Wachstein M. 1947. Nephrotoxic action of dl-serine in the rat. II. The protec- tive action of various amino acids and some other compounds. A rch Pathol 43:515–526. Wagenmakers AJ. 1998. Muscle amino acid metabolism at rest and during exercise: Role in human physiology and metabolism. Exerc Sport Sci Rev 26:287–314. Waisman HA, Harlow HF. 1965. Experimental phenylketonuria in infant monkeys: A high phenylalanine diet produces abnormalities simulating those of the hereditary disease. Science 147:685–695. Wang JML, Creel DJ, Wong KC. 1989. Transurethral resection of the prostate, serum glycine levels, and ocular evoked potentials. Anesthesiology 70:36–41. Waterlow JC. 1969. The assessment of protein nutrition and metabolism in the whole animal, with special reference to man. In: Munro HN ed. Mammalian Protein Metabolism, Vol III. New York: Academic Press. Pp. 347–348. Waterlow JC. 1984. Protein turnover with special reference to man. Quart J Exp Physiol 69:409–438. Waterlow JC, Garlick PJ, Millward DJ. 1978. Protein Turnover in Mammalian Tissues and in the Whole Body. Amsterdam: North-Holland Publishing. Webber WA, Brown JL, Pitts RF. 1961. Interactions of amino acids in renal tubular transport. Am J Physiol 200:380–386. White TP, Brooks GA. 1981. [U-14C]glucose, -alanine, and -leucine oxidation in rates at rest and two intensities of running. Am J Physiol 240:E155–E165.
OCR for page 766
766 DIETARY REFERENCE INTAKES Widdowson EM, Dickerson JWT. 1964. Chemical composition of the body. In: Comar CL, Bronner F, eds. Mineral Metabolism: An Advanced Treatise, Vol 2. New York: Academic Press. Wilcken DE, Reddy SG, Gupta VJ. 1983. Homocysteinemia, ischemic heart disease, and the carrier state for homocystinuria. Metabolism 32:363–370. Wilkin JK. 1986. Does monosodium glutamate cause flushing (or merely “glutamania”)? J Am Acad Dermatol 15:225–230. Willard MD, Gilsdorf RB, Price RA. 1980. Protein-calorie malnutrition in a commu- nity hospital. J Am Med Assoc 243:1720–1722. Williams GM, Whysner J. 1996. Epigenetic carcinogens: Evaluation and risk assess- ment. Exp Toxicol Pathol 48:189–195. Wilson DC, Pencharz PB. 1997. Nutritional care of the chronically ill. In: Tsang RC, Zlotkin SH, Nichols BL, Hansen JW, eds. Nutrition During Infancy: Birth to 2 Years. Cincinnati: Digital Educational Publishing, Inc. Pp. 37–56. Wilson D, Rafii M, Ball RO, Pencharz PB. 2000. Threonine requirement in young men determined by indicator amino acid oxidation with use of L-[1-13C]- phenylalanine. Am J Clin Nutr 71:757–764. Woessner KM, Simon RA, Stevenson DD. 1999. Monosodium glutamate sensitivity in asthma. J Allergy Clin Immunol 104:305–310. Woods RK, Weiner JM, Thien F, Abramson M, Walters EH. 1998. The effects of monosodium glutamate in adults with asthma who perceive themselves to be monosodium glutamate-intolerant. J Allergy Clin Immunol 101:762–771. Wurtman JJ, Wurtman RJ, Growdon JH, Henry P, Lipscomb A, Zeisel SH. 1981. Carbohydrate craving in obese people: Suppression by treatments affecting serotoninergic transmission. Int J Eating Disord 1:2–15. Wynn M, Wynn A. 1979. Prevention of Handicap and the Health of Women. London: Routledge and Kegan Paul. Pp. 43–81. Yamashita K, Ashida K. 1971. Effect of excessive levels of lysine and threonine on the metabolism of these amino acids in rats. J Nutr 101:1607–1614. Yanez E, Uauy R, Ballester D, Barrera G, Chavez N, Guzman E, Saitua MT, Zacarias I. 1982. Capacity of the Chilean mixed diet to meet the protein and energy requirements of young adult males. Br J Nutr 47:1–10. Yang WH, Drouin MA, Herbert M, Mao Y, Karsh J. 1997. The monosodium glutamate symptom complex: Assessment in a double-blind, placebo-controlled, random- ized study. J Allergy Clin Immunol 99:757–762. Yeatman TJ, Risley GL, Brunson ME. 1991. Depletion of dietary arginine inhibits growth of metastatic tumor. Arch Surg 126:1376–1382. Yogman MW, Zeisel SH. 1983. Diet and sleep patterns in newborn infants. N Engl J Med 309:1147–1149. Yogman MW, Zeisel SH. 1985. Nutrients, neurotransmitters and infant behavior. Am J Clin Nutr 42:352–360. Yonetani S, Ishii H, Kirimura J. 1979. Effect of dietary administration of monoso- dium L-glutamate on growth and reproductive functions in mice. Oyo Yakuri (Pharmacometrics) 17:143–152. Young SN. 1986. The clinical psychopharmacology of tryptophan. In: Wurtman RJ, Wurtman JJ, eds. N utrition and the Brain, V ol. 7. New York: Raven Press. Pp. 49–88. Young SN, Gauthier S. 1981. Effect of tryptophan administration on tryptophan, 5- hydroxyindoleacetic acid and indoleacetic acid in human lumbar and cister- nal cerebrospinal fluid. J Neurol Neurosurg Psychiatry 44:323–327.
OCR for page 767
767 P ROTEIN AND AMINO ACIDS Young VR. 1987. 1987 McCollum Award Lecture. Kinetics of human amino acid metabolism: Nutritional implications and some lessons. A m J Clin Nutr 46:709–725. Young VR, Borgonha S. 2000. Nitrogen and amino acid requirements: The Massa- chusetts Institute of Technology Amino Acid Requirement Pattern. J Nutr 130:1841S–1849S. Young VR, Pellett PL. 1990. Current concepts concerning indispensable amino acid needs in adults and their implications for international nutrition plan- ning. Food Nutr Bull 12:289–300. Young VR, Pellett PL. 1994. Plant proteins in relation to human protein and amino acid nutrition. Am J Clin Nutr 59:1203S–1212S. Young VR, Hussein MA, Scrimshaw JS. 1968. Estimate of loss of labile body nitro- gen during acute protein deprivation in young adults. Nature. 218:568–569. Young VR, Tontisirin K, Ozalp I, Lakshmanan F, Scrimshaw NS. 1972. Plasma amino acid response curve and amino acid requirements in young men: Valine and lysine. J Nutr 102:1159–1169. Young VR, Taylor YS, Rand WM, Scrimshaw NS. 1973. Protein requirements of man: Efficiency of egg protein utilization at maintenance and sub-maintenance levels in young men. J Nutr 103:1164–1174. Young VR, Fajardo L, Murray E, Rand WM, Scrimshaw NS. 1975a. Protein requirements of man: Comparative nitrogen balance response within the submaintenance-to-maintenance range of intakes of wheat and beef proteins. J Nutr 105:534–542. Young VR, Steffee WP, Pencharz PB, Winterer JC, Scrimshaw NS. 1975b. Total human body protein synthesis in relation to protein requirements at various ages. Nature 253:192–194. Young VR, Puig M, Queiroz E, Scrimshaw NS, Rand WM. 1984. Evaluation of the protein quality of an isolated soy protein in young men: Relative nitrogen requirements and effect of methionine supplementation. A m J Clin Nutr 39:16–24. Young VR, Gucalp C, Rand WM, Matthews DE, Bier DM. 1987. Leucine kinetics during three weeks at submaintenance-to-maintenance intakes of leucine in men: Adaptation and accommodation. Hum Nutr Clin Nutr 41:1–18. Young VR, Bier DM, Pellett PL. 1989. A theoretical basis for increasing current estimates of the amino acid requirements in adult man, with experimental support. Am J Clin Nutr 50:80–92. Young VR, Marchini JS, Cortiella J. 1990. Assessment of protein nutritional status. J Nutr 120:1496–1502. Young VR, Wagner DA, Burini R, Storch KJ. 1991. Methionine kinetics and bal- ance at the 1985 FAO/WHO/UNU intake requirement in adult men studied with L-[2H3-methyl-1-13C]methionine as a tracer. Am J Clin Nutr 54:377–385. Young VR, El-Khoury AE, Raguso CA, Forslund AH, Hambraeus L. 2000. Rates of urea production and hydrolysis and leucine oxidation change linearly over widely varying protein intakes in healthy adults. J Nutr 130:761–766. Yuwiler A, Brammer GL, Morley JE, Raleigh MJ, Flannery JW, Geller E. 1981. Short- term and repetitive administration of oral tryptophan in normal men. Effects on blood tryptophan, serotonin, and kynurenine concentrations. Arch Gen Psychiatry 38:619–626. Zanni E, Calloway DH, Zezulka AY. 1979. Protein requirements of elderly men. J Nutr 109:513–524.
OCR for page 768
768 DIETARY REFERENCE INTAKES Zello GA, Pencharz PB, Ball RO. 1990. Phenylalanine flux, oxidation and conver- sion to tyrosine in humans studied with L-[1-13C]phenylalanine. Am J Physiol 259:E835–E843. Zello GA, Pencharz PB, Ball RO. 1993. Dietary lysine requirement of young adult males determined by oxidation of L-[1-13C]phenylalanine. A m J Physiol 264:E677–E685. Zello GA, Wykes LJ, Ball RO, Pencharz PB. 1995. Recent advances in methods of assessing dietary amino acid requirements for adult humans. J Nutr 125:2907– 2915. Zezulka AY, Calloway DH. 1976a. Nitrogen retention in men fed isolated soybean protein supplemented with L-methionine, D-methionine, N-acetyl-L-methionine, or inorganic sulfate. J Nutr 106:1286–1291. Zezulka AY, Calloway DH. 1976b. Nitrogen retention in men fed varying levels of amino acids from soy protein with or without added L-methionine. J Nutr 106:212–221. Zhao X-H, Wen ZM, Meredith CN, Matthews DE, Bier DM, Young VR. 1986. Threonine kinetics at graded threonine intakes in young men. Am J Clin Nutr 43:795–802. Ziegler TR, Benfell K, Smith RJ, Young LS, Brown E, Ferrari-Baliviera E, Lowe DK, Wilmore DW. 1990. Safety and metabolic effects of L-glutamine administra- tion in humans. J Parenter Enteral Nutr 14:137S–146S. Zimmerman FT, Burgemeister BB. 1959. A controlled experiment of glutamic acid therapy. AMA Arch Neurol Psych 81:639–648. Zlotkin SH. 1989. Nutrient interactions with total parenteral nutrition: Effect of histidine and cysteine intake on urinary zinc excretion. J Pediatr 114:859–864.
Representative terms from entire chapter: