Article

Effects of D-, DL-and L-glutamic acid on chicks

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Abstract

Studies were conducted to investigate the effects of D-, DL-, or L-glutamic acid on the chick. Supplementation of levels of L-glutamic acid to an amino acid mixture containing adequate levels of all the indispensable amino acids plus cystine and tyrosine resulted in increased growth up to 10% L-glutamic acid in the diet. Chicks tolerated as much as 15% L-glutamic acid with no growth retardation. Supplementation of D-glutamic acid at levels of 3.75 or 5% resulted in growth depressions of 18 and 38%, respectively, at the end of a 2-week experiment. Significant growth-depressing effects of these levels of D-glutamic acid and 7.5% of DL-glutamic acid were also observed with an amino acid diet as well as an isolated soybean protein diet. The growth-depressing effect was most severe during week 2 of the experiment. Additional vitamins and amino acid supplements failed to reverse the growth-depressing effect. Plasma glutamic acid concentration was not altered by the inclusion of D-glutamic acid in the diet, but generally, plasma free amino acid concentrations were increased. This was especially true of arginine. Free glutamic acid increased in the kidney and was lowered in the liver. Free ammonia was increased in both the liver and kidney when the D form was included in the diet. Implications of these findings are discussed.

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... L-glutamic acid, L-alanine and glycine were the amino acid supplements chosen, and DAC was used as the NPN supplement. Maruyama et al. (1975) supplemented chick diets with up to 10% of L-glutamic acid, and did not observe any decline in food consumption. Addition of 3% L-alanine (Maruyama et al., 1975) or 1.6% glycine (Lee et al., 1972) to a semipurified basal diet also did not depress food consumption by chicks. ...
... Maruyama et al. (1975) supplemented chick diets with up to 10% of L-glutamic acid, and did not observe any decline in food consumption. Addition of 3% L-alanine (Maruyama et al., 1975) or 1.6% glycine (Lee et al., 1972) to a semipurified basal diet also did not depress food consumption by chicks. Davis and Austic (1997) did report a decrease in food consumption in chicks over a 9 d period when 4% ...
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After obtaining a cDNA clone for chicken hepatic histidase, experiments were conducted to study the regulation of histidase mRNA expression by dietary protein concentrations. Histidase mRNA expression was increased within 3 h when chicks consumed higher levels of dietary protein. Increasing the dietary concentration of histidine did not alter hepatic histidase mRNA expression. The rapid increase in histidase mRNA levels in response to dietary protein intake is similar to the rapid decrease seen in malic enzyme mRNA levels in chicks fed the high protein diets. Glucagon was shown to regulate the mRNA expression of both the enzymes, and could act as a mediator for the effect of dietary protein on histidase and malic enzyme mRNA expression since an increase in dietary protein intake elevated plasma glucagon concentration within 1 h. While histidase mRNA expression seems to be regulated by concentrations of specific amino acids in the diet, malic enzyme mRNA expression seems to be regulated by the total protein or nitrogen level of the diet. Finally, addition of synthetic glutamic acid to a practical corn-soy poultry diet reduced the amount of abdominal fat present in broiler chicks at slaughter. Thesis (Ph. D.)--University of Georgia, 2003. Directed by Adam J. Davis. Includes bibliographical references (leaves 103-116). Electronic reproduction. s
... Compared to D-Asp, the information for D-Glu is limited. Maruyama et al. (1975) reported that chicks derived from mating male New Hampshire with female Single Comb White Leghorn, tolerated nearly 15% of dietary L-Glu with no growth retardation. However, 3.75% of D-Glu levels resulted in growth suppression at the end of the 2-week experiment. ...
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D-Amino acids occur in modest amounts in bacterial proteins and the bacterial cell wall, as well as in peptide antibiotics. Therefore, D-amino acids present in terrestrial vertebrates were believed to be derived from bacteria present in the gastrointestinal tract or fermented food. However, both exogenous and endogenous origins of D-amino acids have been confirmed. Terrestrial vertebrates possess an enzyme for converting certain L-isomers to D-isomers. D-Amino acids have nutritional aspects and functions, some are similar to, and others are different from those of L-isomers. Here, we describe the nutritional characteristics and functions of D-amino acids and also discuss the future perspectives of D-amino acid nutrition in the chicken.
... But these early studies clearly illustrate that a certain amount of dietary non-essential amino acids are required (Rechcigl et al., 1957) and that glutamate may be the ideal source. Indeed a number of studies were carried out that claimed dietary glutamate could be considered essential for growth in a variety of species, such as the chicken (Featherson et al., 1962;Maruyama et al., 1975Maruyama et al., , 1976. However, the fact that dietary glutamate is unlikely to be limiting meant that interest in such work was considered of limited practical application and the topic received little attention over the past 30-40 years. ...
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... Such early studies clearly illustrate that a certain amount of dietary non-essential amino acids are required and that glutamate may be the ideal source (Featherston et al., 1962). A number of studies were carried out that claimed dietary glutamate could be essential for growth in chickens (Maruyama et al., 1975(Maruyama et al., , 1976, and it has been proposed that glutamine is limiting for milk production in the cow (Meijer et al., 1993(Meijer et al., , 1995, but overall, the use of dietary glutamate/glutamine has received very little attention over the past 50 years. But, despite having been classified as non-essential, there is increasing evidence that supplemental glutamate/glutamine may be beneficial, not only in hypercatabolic states, but also in the maintenance of optimal health and maximal rates of growth in healthy animals. ...
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... In contrast, free Glu concentration in plasma did not change among all groups. Previous studies using pigs (Reeds et al., 1996) and chicks (Maruyama et al., 1975) showed that plasma Glu concentration was not altered by dietary Glu. From the aforementioned results, it was concluded that most of the dietary Glu was used for energy production in intestines (Reeds et al., 1996). ...
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The addition of 1% dl-phenylalanine and 1% l(-) tyrosine to a purified diet containing 10% casein produced growth retardation and external lesions. Phenylalanine is converted to tyrosine in the animal and so may add to the effect of the tyrosine. The addition of relatively large amounts of nicotinic acid or l(-)tryptophane will appre ciably alleviate the deleterious effects of these amino acids.
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1. Hypertryptophanaemia, hypertryptophanuria and to a lesser degree a generalized hyperaminoaciduria were observed in phenylketonuric patients receiving certain commercial low-phenylalanine diets containing DL-tryptophan. 2. The generalized hyperaminoaciduria was associated with the ingestion of acid hydro-lysates of protein, but not with the ingestion of enzymic hydrolysates or D-tryptophan. 3. Alanine recovered from the urine of these treated patients had a D-isomer content of approx. 50%. This amount of urinary D-alanine could be derived from the ingestion of an acid hydrolysate of protein in which the amino acids had racemized to the extent of 2–3%.
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In the normal fasted dog ammonia was added to the blood in the kidneys and portal bed and was removed in the liver. Glycine given intravenously resulted in ammonia release into the blood in the liver and additional ammonia release by the kidneys, with concomitant rise in the arterial ammonia concentration. At high arterial levels ammonia was removed in the extremities and head. l-Arginine injected intravenously during the glycine infusion produced an abrupt cessation of ammonia release by the liver and caused this organ to remove ammonia from the incoming blood. A rapid fall in arterial ammonia concentration occurred. Arginine did not affect ammonia release or removal by any organ tested other than the liver. The possible therapeutic significance of the capacity of l-arginine to prevent ammonia release at an important site of ammonia formation is discussed.
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The toxicity of 19 amino acids when fed individually in excess (5% level) in a low-protein diet was studied with weanling rats. With the exception of alanine, all amino acids tested produced depressions in growth to varying degrees. Methionine produced the severest growth depressions followed in decreasing order by tryptophan, DL-aspartic acid, histidine, tyrosine, phenylalanine, cystine, leucine, valine, isoleucine, glycine, asparagine, arginine, L-aspartic acid, lysine and threonine. Glutamic acid, proline and serine produced only slight growth depressions. Results of studies on the isomers of several amino acids indicated that the D-isomers usually produced less inhibition in growth than the corresponding L-form. DL-Aspartic acid, however, produced greater detrimental effects than L-aspartic acid. The growth depression of the several amino acids studied could be partially or completely prevented by supplements of protein to the diet. The degree of toxicity of the amino acids was dependent also upon the specific protein fed the animals. L-Cystine at a level of 5% in a low-protein diet depressed growth and produced some deaths. When the casein in the high-cystine diet was increased to a level of 36%, the number of deaths was greatly increased. When lactalbumin was fed in place of casein, however, no deaths occurred and growth was nearly normal. Supplements of leucine or of hemoglobin to a corn grain basal diet produced a severe depression in growth. The effect was partially-to-completely reversed by supplements of isoleucine. Analyses of the plasma usually demonstrated high values for free amino acid content of the amino acid supplemented in excess in the diet. However, the toxicity of several amino acids did not appear to be directly related to their plasma concentration.
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• Levels of methionine only slightly above those necessary for growth depressed the growth of rats fed limiting amounts of vitamin B6. Vitamin B6 counteracted the effects of moderate amounts of methionine. When the diet contained 2.5% of methionine, high levels of the vitamin failed to restore growth. D-, L- and DL-methionine and DL-homocystine were approximately equivalent in depressing growth; cystine did not depress growth. • Acrodynia was aggravated by moderate amounts of methionine (D-, L- or DL-isomers), and by homocystine. • Glycine, alanine, serine, cystine, threonine, and additional B vitamins did not affect growth when moderate levels of methionine were added to diets limiting or deficient in vitamin B6. • When the ration contained 1.0% of added methionine, the three forms of vitamin B6 were approximately equal in promoting growth; in some experiments the most active form of the vitamin appeared to be pyridoxal. • The consumption of pyridoxine decreased the excretion of free methionine in the urine of rats fed moderate amounts of the amino acid. Dietary methionine did not affect the concentration of vitamin B6 in the blood or liver of rats.
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• Addition of 3, 6, and 9% glycine to vitamin B12-deficient diets caused a growth depression and increased mortality in growing chickens. • Both vitamin B12 and folic acid function in counteracting this toxicity; however, B12 is somewhat more effective. • Addition of 6 or 9% glycine to the diet increased blood uric acid levels. Folic acid tended to decrease these high levels of uric acid in the blood. • Vitamin B12 tends to increase the level of uric acid in the blood of young chickens.
Determination tamic acids by enzymatic
  • A Meister
  • Sober
Meister,A., Sober, (1951) Determination tamic acids by enzymatic Biol. Chem.189, 591-595.
& Kukuchi cance of the glycine cleavage cine andserine catabolism
  • T Yoshida
Yoshida, T. & Kukuchi cance of the glycine cleavage cine andserine catabolism Arch. Biochem. Biophys. 145, 658-668.
Growth corneal vascularization phenylalaninein a purified Effect of excess dietary H acid requirement amino of acid nitro diet Effect requirement. of glutamic Poultry H.A. & Tice, of aspartic decarboxylationPrin of Statistics
  • C F Niven
  • Jr
  • G A T F Washburn
  • R Bird
  • M L L Sunde
Niven, C. F., Jr., Washburn, G.A. (1946)Growth corneal vascularization phenylalaninein a purified Exp. Biol. Med. 63, 106-108. T. F., Bird, Effect of excess dietary H. R. & Sunde,M. L. L-, DL- and B. C. acid requirement amino of acid nitro diet. J. Nutr. 78, Effect requirement. of glutamic Poultry H.A. & Tice, of aspartic decarboxylation. S. V. glu and J. ( 1960)Prin of Statistics.McGraw-G.(1971) system in gly inavian Signifi liver. Toxicityof amino deficiency. M. R. & Sperling retardation with tyrosine diet. and and Soc.Proc. by guest on July 9, 2011 jn.nutrition.org Downloaded from rD-, DL- AND L-GLUTAMICACID FOR CHICKS 1019
dietary aZ-serine in rats
  • Fishman
Fishman, dietary aZ-serine in rats. Proc. Soc. Exp. Biol. Med. 57, 241-243.
Theamino growingchicks fed a crystalline diet
  • G J Klain
  • H M Scott
  • Johnson
Klain, G. J., Scott, H. M. & Johnson, ( 1960 ) Theamino growingchicks fed a crystalline diet. PoultrySci. 39, 39-44.
Isolation mogeneous preparation thetase-L-serine
  • Nagabhushanam
Nagabhushanam, (1965 ) Isolation mogeneous preparation thetase-L-serine J. Biol. Chem. 240, 3002-3008.
the toxicity Some reduceof C. A. be vitaminB« Effect of vita-and uri DentónStudies on the acids forof amino Aminoaciduria administration re in (1968) Effects distribution chim
  • H N Christensen
  • A M W H Cullen
  • C Artom
Christensen, H. N. & Cullen, A. M. W. H. & Artom, C. factorswhich (1944) the toxicity Some reduceof C. A. be vitaminB«.J. Nutr. A. H., Effect of vita-and uri Dentón, (1952) J.L. & Ship,A. G. glycine infusion: J. Lab. Clin. ef 51,Med. (1961)Studies on the acids forof amino Aminoaciduria administration re in (1968) Effects distribution chim. Biophys. Acta 750, 237-252.
C. a-aminoisobutyric in chicks
  • T-C Shao
  • D Hill
Shao, T-C. & Hill, D. C. a-aminoisobutyric in chicks. J. Nutr. 98, 225-234.
D-serine on the chicks
  • Shen
Shen, (1973) D-serine on the chicks. Poultry Sci. 52, 1168- 1174.
Prin ciples and Procedures of Statistics
  • R G D Steel
  • J H Torrie
Steel, R. G. D. & Torrie, J. H. ( 1960) Prin ciples and Procedures of Statistics. McGraw- Hill Book Co., New York.
Isolation and properties of a ho mogeneous preparation of cystathionine synthetase-L-serine and L-threonine dehydratase
J. Biol. Chem. 239, 3357-3360. 21. Nagabhushanam, A. & Greenberg, D. M. ( 1965 ) Isolation and properties of a ho mogeneous preparation of cystathionine synthetase-L-serine and L-threonine dehydratase.
Some dietary factors which reduce the toxicity of aZ-serine in rats
  • W H Fishman
  • C Artom
Fishman, W. H. & Artom, C. (1944) Some dietary factors which reduce the toxicity of aZ-serine in rats. Proc. Soc. Exp. Biol. Med. 57, 241-243.