Amino acids in diet

Kashani, A.B., H. Sarnie, R.J. Emerick, and C.W. Carlson. 1986. Effect of copper with three levels of sulfur containing amino acids in diets for turkeys. Poultry Sci. 65 1754-1759. 

Fleck, A., Shepherd, J., and Munro, H. N., Protein synthesis in rat liver. Influence of amino acids in diet on microsomes and polysomes, Science, 150, 628,1965. 

Nicol, B. M. and Phillips, P. G. (1978). The utilization of proteins and amino acids in diets based on cassava Manihot utilissima), rice sorghum Sorghum sativa) by young Nigerian men of low income. Br. J. Nutr. 39, 271-286. 

Humans are able to synthesize only 11 of the 20 amino acids in proteins, called nonessential amino acids. The other 9, called essential amino acids, are biosynthesized only in plants and microorganisms and must be obtained in our diet. The division between essential and nonessential amino acids is not clearcut, however tyrosine, for instance, is sometimes considered nonessential because humans can produce it from phenylalanine, but phenylalanine itself is essential and must be obtained in the diet. Arginine can be synthesized by humans, but much of the arginine we need also comes from our diet. 

Two amino acids—cysteine and tyrosine—can be synthesized in the body, but only from essential amino acid ptecutsots (cysteine from methionine and tyrosine from phenylalanine). The dietary intakes of cysteine and tytosine thus affect the requirements for methionine and phenylalanine. The remaining 11 amino acids in proteins are considered to be nonessential or dispensable, since they can be synthesized as long as there is enough total protein in the diet—ie, if one of these amino acids is omitted from the diet, nitrogen balance can stiU be maintained. Howevet, only three amino acids—alanine, aspartate, and glutamate—can be considered to be truly dispensable they ate synthesized from common metabolic intetmediates (pyruvate, ox-... 

Yoshiji, H., Nakae, D., Mizumoto, Y., Horiguchi, K., Tamura, K., Denda, A., Tsujii, T. and Konishi, Y. (1992). Inhibitory effect of dietary iron deficiency on inductions of putative preneoplastic lesions as well as 8-hydroxydeoxyguanosine in DNA and lipid peroxidation in the livers of rats caused by exposure to a choline-deficient L-amino acid defined diet. Carcinogenesis 13, 1227-1233. 

Arteel and Sies (1999) examined procyanidin oligomers of different size, isolated from the seeds of Theobroma cacao, for their ability to protect against nitration of tyrosine. Serraino and others (2003) investigated antioxidant activity of the blackberry juice and cyanidin-3-O-glucoside on endothelial dysfunction in cells and in vascular rings exposed to peroxynitrite. However, more work is needed in this area, and the confounding effects of oxidized protein/amino acids in the diet need to be elucidated. 

Consider one small molecule, phenylalanine. It is an essential amino acid in our diet and is important in protein synthesis (a component of protein), as well as a precursor to tyrosine and neurotransmitters. Phenylalanine is one of several amino acids that are measured in a variety of clinical methods, which include immunoassay, fluorometry, high performance liquid chromatography (HPLC see Section 4.1.2) and most recently MS/MS (see Chapter 3). Historically, screening labs utilized immunoassays or fluorimetric analysis. Diagnostic metabolic labs used the amino acid analyzer, which was a form of HPLC. Most recently, the tandem mass spectrometer has been used extensively in screening labs to analyze amino acids or in diagnostic labs as a universal detector for GC and LC techniques. Why did MS/MS replace older technological systems The answer to this question lies in the power of mass spectrometer. 

Characteristically, legume seeds are rich in protein and contain intermediate to high levels of lysine and threonine which are important in balancing the deficiencies of these essential amino acids in cereal diets. Certain legume proteins, such as soybean, also exhibit strong functional properties, especially water solubility, water and fat binding and emulsification. Thus soybean flours, protein concentrates and isolates have been used widely as nutritional supplements and functional ingredients in foods. 

The problem to be solved with respect to the chemical reactions that constitute metabolism and sustain life is that, without the action of catalysts, they are far too slow. Let s consider the digestion of the proteins themselves, an important constituent of our diet. In an enviromnent similar to that of our digestive system, several tens of thousand years would be required to digest half of the protein content of a typical meal in the absence of a catalyst. Clearly, this will not do. In reality, the stomach secretes one protein catalyst, the enzyme pepsin, and the pancreas secretes several enzymes that catalyze the digestion of proteins. In the presence of these enzymes, dietary proteins are fully digested and reduced to their basic constituents, the amino acids, in a matter of hours. Obviously, these enzymes are enormously potent catalysts." ... 

The amonnt of protein synthesised and then released in (iv) and (v) is abont 70 g each day. Even under conditions of starvation or malnutrition, proliferation and differentiation of stem cells located in the crypts of the villi are important to provide the cells necessary for replenishment of those lost from the villi. New cells move up the villus to replace those lost at the top. Under these conditions, amino acids are not available from the intestine and have to be taken up from the blood across the basolateral membrane. A low level of amino acids in the blood, due to chronic malnutrition, will prevent or reduce the rate of proliferation of these cells, so that digestion of even the small amount of food ingested during malnutrition, or refeeding after starvation, is difficult. A vicious circle thus results from protein-deficient diets which increase the risk of development of protein-energy-malnutrition. This is especially severe in children but may also contribute to the clinical problems that occur in the elderly whose diets are of low quality. 

Experiments with rats have shown that the branched-chain a-keto acid dehydrogenase complex is regulated by covalent modification in response to the content of branched-chain amino acids in the diet. With little or no excess dietary intake of branched-chain amino acids, the enzyme complex is phosphorylated and thereby inactivated by a protein kinase. Addition of excess branched-chain amino acids to the diet results in dephosphoiylation and consequent activation of the enzyme. Recall that the pyruvate dehydrogenase complex is subject to similar regulation by phosphorylation and dephosphorylation (p. 621). 

D. Cysteine is an essential amino acid in individuals consuming a diet devoid of methionine. 

All the amino acids that eventually appear in the finished protein must be present at the time of protein synthesis. [Note If one amino acid is missing (for example, if the diet does not contain an essential amino acid), that amino acid is in limited supply in the cell, and translation, therefore, stops at the codon specifying that amino acid. This demonstrates the importance of having all the essential amino acids in sufficient quantities in the diet to ensure continued protein synthesis (see p. 259 for a discussion of the essential amino acids).]... 

Of the 20 amino acids the human body uses to build proteins, the adult body is able to produce 12 of them in amounts sufficient for its needs—it produces these amino acids from carbohydrates and fatty acids. The remaining 8, listed in Table 13.6, must be obtained from food. Because the body needs these eight amino acids but cannot synthesize them, they are called essential amino acids, in the sense that it is essential we get adequate amounts of them from our food. To support rapid growth, infants and children require, in addition to the eight amino acids listed for adults in Table 13.6, large amounts of arginine and histidine, which can be obtained only from the diet. Infants and juveniles therefore have a total of 10 essential amino acids. (The term essential is unfortunate because, in truth, all 20 amino acids are vital to our good health.)... 

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