The Amino Acids Required for Growth in Mice and the Availability of their Optical Isomers

Bauer, Clifford D.; Berg, Clarence P.

doi:10.1093/jn/26.1.51

Cited by 64 publications

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“…The only isoleucine in the essential amino acid mixture ,used was part of an «I-leucine-isoleucine mixture" of unstated composItion. The marked loss in weight of all rats fed the essential amino aci<i mixture is in striking contrast with the experiences of others (13,17,27) with essential acid mixtures which contained racemic amino acids in similar proportions. The possible existence of an overshadowing deficiency in the diet was not investigated, nor was any attempt made to verify or account for the reported nitrogen re tentions of 0.154 to 0.381 gm.…”

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confidence: 78%

“…The nine amino acids required for growth in the rat appear to be indispensable also in the mouse (17). Since removal of arginine from the dietary mixture of twenty purified amino acids did not retard growth, the capacity of the mouse to synthesize arginine was probably appreciable; inasmuch, however, as weight increments on the complete mixtures were sub-maximal, the evidence was inadequate to establish dispensability for maximum growth.…”

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confidence: 99%

“…The d modifications of methionine and phenylalanine were avail able to the mouse for growth, but the d isomers of valine, leucine, isoleucine, and threonine were not (17). Isotopic d-Iysine with NU in the a-amino group and deuterium in the �, 'V, and � positions was added in small amounts daily for f o ur days to the stock diet fed grow ing rats.…”

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confidence: 99%

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The Metabolism of Proteins and Amino Acids

Berg¹

1944

Annu. Rev. Biochem.

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In the compilation of this review an attempt has been made to give appropriate recognition· to the current interest in normal and emer gency nutrition, by discussing such aspects as the amino acid needs of the human subject, the synthesis of blood proteins, intravenous ali mentation, and the use of urea by ruminants. References to papers in the fields of plant and bacterial metabolism have been largely omitted. During the year many delayed foreign journals have become available, but their arrival has been erratic and it has not been possible to fill some of the gaps. Throughout the review 1 and d have been used in the configurational sense.Essential amino acids.-The amino acid requirements for main tenance in the adult human subject have recently been tested with protein hydrolyzates and with mixtures of purified amino acids as the chief or sole source of protein nitrogen. Studies of the former type have come chiefly from the laboratory of Holt. Nitrogen equilibrium was readily maintained on an enzymic hydrolyzate of casein, but this was not possible with acid-hydrolyzed casein until tryptophan . �had been added (1, 2). Two other acid hydrolyzates were prepared, one from casein which had been deaminized to destroy the lysine (3) and the other from casein which had been oxidized with hydrogen perox ide (4, 5) to convert the methionine to the corresponding biologically inactive sulfone (6) which was removed as the insoluble calcium sul fonate. From the latter preparation most of the residual cystine was also removed by adsorption on norit. When the former hydrolyzate was fed in diets fortified with tryptophane, equilibrium was not at tained until lysine was added (7, 8). Supplementation of the latter hydrolyzate with tryptophane, methionine, and cystine provided a mix ture adequate for maintenance. Removal of the methionine produced negative nitrogen balances and loss of body weight; its restoration re-established nitrogen equilibrium in a few days, but did not increase the body weight. 0 The inconsistent results obtained by the omission of cystine were considered to suggest that cystine was essential, but this conclusion was t.bought to require confirmation (9). An abstract 239 Annu. Rev. Biochem. 1944.13:239-262. Downloaded from www.annualreviews.org Access provided by Technische Universiteit Eindhoven on 02/02/15. For personal use only.Quick links to online content Further ANNUAL REVIEWS

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The Metabolism of Proteins and Amino Acids

Berg¹

1944

Annu. Rev. Biochem.

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“…In mice, early observations indicated that this species was able to synthesize arginine (14), but it was not clear if this endogenous source of arginine was sufficient to meet the demand for this amino acid. Current dietary arginine recommendations [3-g/kg diet (15)] are based on the work of John and Bell (16,17).…”

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confidence: 99%

Dietary Arginine Requirements for Growth Are Dependent on the Rate of Citrulline Production in Mice

Marini

Agarwal

Didelija

2015

The Journal of Nutrition

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“…In experimental animals, tryptophan deficiency can lead to a disturbance in growth [Willcock and Hopkins, 1906]. Tryptophan is required for the maintenance of nitrogen equilibrium in mature rats [Nasset and Ely, 1953], mice [Bauer and Berg, 1943], pigs [Mertz et al, 1952], and dogs [Rose and Rice, 1939]. Animals subjected to tryptophan deficiency can cause some maladies such as cataracts [Totter and Day, 1942;Ferraro and Roizin, 1947] and corneal vascularization [Sydenstricker et al, 1947].…”

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confidence: 99%

Possible roles of excess tryptophan metabolites in cancer

Chung

Gadupudi

2011

Environ and Mol Mutagen

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Tryptophan is metabolized through serotonin, indole, and kynurenine (KN) pathways. Uptake of an excess amount of tryptophan accompanied with vitamin B6 deficiency may result in the accumulation of higher concentrations of metabolites mainly from the KN pathways in the bladder. These metabolites could interact with nitrite to become mutagenic nitrosamines. They could be a promoter in the initiator-promoter model of carcinogenesis. They produced bladder cancer when implanted in the bladder. They also interact with transition metals copper or iron to form reactive radicals or reactive oxygen species (ROS). Some metabolites, 3-hydroxy-anthranilic acid, were autooxidized to mutagenic cinnabarinic and anthranilyl radical intermediates. These radical intermediates could also be ligands that interact with aryl hydrocarbon receptor (AhR) and induce xenobiotic metabolizing enzymes (XMEs) to metabolize contaminated carcinogens. When tryptophan is exposed to either visible or UV light, a photoproduct of 6-formylindolo[3,2b]-carbazole is formed, which has a very high affinity for the AhR that plays a role in carcinogenesis. This review gives an insight into various mechanisms through which tryptophan metabolites cause carcinogenesis. It could be concluded that tryptophan metabolites play a complementary role in promoting carcinogenesis along with carcinogens like aflatoxin, CCl(4) , 2-acetylaminofluorene, 4-aminobiphenyl, 2-naphthylamine, or N-[4-(5-nitro-2-furyl)-2-thiazolyl] formamide. The underlying mechanisms could be their autoxidation, exposure to either visible or UV light, interaction with nitrite or transition metals to form reactive intermediates, serving as ligands to interact with an AhR that is known to play a role in carcinogenesis through induction of XMEs. Further research is warranted.Environ.

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The Amino Acids Required for Growth in Mice and the Availability of their Optical Isomers

Cited by 64 publications

References 39 publications

The Metabolism of Proteins and Amino Acids

The Metabolism of Proteins and Amino Acids

Dietary Arginine Requirements for Growth Are Dependent on the Rate of Citrulline Production in Mice

Possible roles of excess tryptophan metabolites in cancer

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