Effects in vivo and in vitro of l-glutamic acid-γ-hydrazide on metabolism of some free amino acids in brain and liver

1966 ◽  
Vol 15 (11) ◽  
pp. 1831-1845 ◽  
Author(s):  
Ricardo Tapia ◽  
Herminia Pasantes ◽  
Berta G. Ortega ◽  
Guillermo H. Massieu
1971 ◽  
Vol 124 (2) ◽  
pp. 385-392 ◽  
Author(s):  
R. W. Wannemacher ◽  
C. F. Wannemacher ◽  
M. B. Yatvin

Weanling (23-day-old) rats were fed on either a low-protein diet (6% casein) or a diet containing an adequate amount of protein (18% casein) for 28 days. Hepatic cells from animals fed on the deficient diet were characterized by markedly lower concentrations of protein and RNA in all cellular fractions as compared with cells from control rats. The bound rRNA fraction was decreased to the greatest degree, whereas the free ribosomal concentrations were only slightly less than in control animals. A good correlation was observed between the rate of hepatic protein synthesis in vivo and the cellular protein content of the liver. Rates of protein synthesis both in vivo and in vitro were directly correlated with the hepatic concentration of individual free amino acids that are essential for protein synthesis. The decreased protein-synthetic ability of the ribosomes from the liver of protein-deprived rats was related to a decrease in the number of active ribosomes and heavy polyribosomes. The lower ribosomal content of the hepatocytes was correlated with the decreased concentration of essential free amino acids. In the protein-deprived rats, the rate of accumulation of newly synthesized cytoplasmic rRNA was markedly decreased compared with control animals. From these results it was concluded that amino acids regulate protein synthesis (1) by affecting the number of ribosomes that actively synthesize protein and (2) by inhibiting the rate of synthesis of new ribosomes. Both of these processes may involve the synthesis of proteins with a rapid rate of turnover.


1987 ◽  
Vol 252 (4) ◽  
pp. R768-R773
Author(s):  
M. A. Lang

The euryhaline crab, Callinectes sapidus, behaves both as an osmoregulator when equilibrated in salines in the range of 800 mosM and below and an osmoconformer when equilibrated in salines above 800 mosM. There exists a close correlation between osmoregulation seen in the whole animal in vivo and cell volume regulation studied in vitro. Hyperregulation of the hemolymph osmotic pressure and cell volume regulation both occurred in salines at approximately 800 mosM and below. During long-term equilibration of the crabs to a wide range of saline environments, the total concentration of hemolymph amino acids plus taurine remained below 3 mM. During the first 6 h after an acute osmotic stress to the whole animal, the hemolymph osmotic pressure and Na activity gradually decreased, whereas the free amino acids remained below 3 mM. As the hemolymph osmotic pressure decreased below approximately 850 mosM, the amino acid level began to increase to 17-25 mM. This change was primarily due to increases in glycine, proline, taurine, and alanine. The likely source of the increase in hemolymph free amino acids in vivo is the free amino acid loss from muscle cells observed during cell volume regulation in vitro.


1972 ◽  
Vol 43 (6) ◽  
pp. 823-837 ◽  
Author(s):  
D. Burston ◽  
Jill M. Addison ◽  
D. M. Matthews

1. The characteristics of transport and hydrolysis of twenty-two dipeptides containing basic and acidic amino acids by rat ileal rings were investigated in vitro. The peptides included combinations of basic and neutral, basic and basic, basic and acidic, acidic and acidic, and acidic and neutral amino acids. 2. All peptides studied were removed intact from the bulk phase of the incubation medium, though, in general, only free amino acids appeared in the tissue. Uptake of one or both constituent amino acids was greater from the peptide than from the equivalent amino acid or amino acid mixture in the case of at least one peptide from each group and in eighteen of the twenty-two peptides studied. In general, there was no relationship between the extent of uptake of amino acids from peptides and the extent of their hydrolysis by the system. The results support the hypothesis that there is more than one mode of uptake of amino acids from peptides. 3. Hydrolysis of γ-glutamyl-l-glutamic acid by intact intestine or intestinal homogenate was slight, and intact peptide was taken up by the tissue. Uptake of free glutamic acid from this peptide was poor. Comparison of γ-glutamyl-l-glutamic acid with three other slowly hydrolysed dipeptides, glycyl-d-valine, sarcosylglycine and glycylsarcosine, suggested that all four were transported into the mucosal cells and hydrolysed intracellularly. The results indicate that the presence of a γ-linkage or a d-amino acid, or methylation of the free amino group as in sarcosylglycine, impair both transport and hydrolysis of peptide, but that attachment of a methyl group to the N of the peptide bond, as in glycylsarcosine, impairs hydrolysis but has no effect on peptide transport. 4. l-Aspartic acid and l-glutamic acid were extensively transaminated by the intestine, whether presented as free amino acids or in peptides. Evidence was obtained suggesting that production of alanine from aspartic acid resulted from direct transamination of aspartic acid with pyruvic acid, rather than from a sequence of two reactions involving aspartate and alanine aminotransferases. 5. The results show that more rapid uptake of amino acids from peptides than from free amino acids is not confined to peptides made up of neutral amino acids, and probably occurs with many small peptides. Uptake of lysine and the dicarboxylic amino acids, which are particularly slowly absorbed from free solution, was much greater from several dipeptides than from the free amino acids. The results suggest the importance of mucosal peptide uptake in protein absorption.


1974 ◽  
Vol 46 (3) ◽  
pp. 393-402 ◽  
Author(s):  
D. B. A. Silk ◽  
D. Perrett ◽  
Joan P. W. Webb ◽  
M. L. Clark

1. A double-lumen perfusion technique has been used in man to study intestinal absorption of two tripeptides, glycyl-glycyl-glycine and l-alanyl-glycyl-glycine. Intraluminal tripeptide hydrolysis has been investigated by incubating both tripeptides in vitro with fresh uncentrifuged saline aspirates. 2. Glycine was absorbed faster from a glycyl-glycyl-glycine solution (3·3 mmol/l) than from an equivalent (10 mmol/l) glycine solution, and both l-alanine and glycine were absorbed faster from 10 mmol/l l-alanyl-glycyl-glycine than from the equivalent amino acid mixture. Free amino acids and dipeptides were aspirated during the tripeptide perfusions. 3. l-Alanyl-glycyl-glycine was hydrolysed faster than glycyl-glycyl-glycine in vitro, and results indicated that hydrolysis of the tripeptides occurred from the N-terminal end of the molecule. Intraluminal tripeptide hydrolysis was not sufficient to account for the concentrations of free amino acids and dipeptides liberated during the tripeptide perfusion experiments in vivo. 4. It is suggested that the liberated amino acids and dipeptides either diffused back into the luminal contents after hydrolysis in the brush border had taken place, or effluxed from the mucosal cell after intracellular tripeptide hydrolysis.


1980 ◽  
Vol 238 (1) ◽  
pp. E46-E52
Author(s):  
S. L. Augustine ◽  
R. W. Swick

The recovery of approximately 40% of the total liver protein during the first day after partial hepatectomy was shown to be due to the near cessation of protein breakdown rather than to an increase in protein synthesis. The decrease in degradation of total protein was less if rats were adrenalectomized or protein-depleted prior to partial hepatectomy. The effect of these treatments originally suggested that changes in free amino acid levels in liver might be related to the rate of protein degradation. However, no correlation was found between levels of total free amino acids and rates of breakdown. Measurements of individual amino acids during liver regeneration suggested that levels of free methionine and phenylalanine, amino acids that have been found to lower rates of protein degradation in vitro, are not correlated with rates of breakdown in vivo. The difference between the fractional rate of ornithine aminotransferase degradation (0.68/day and 0.28/day in sham-hepatectomized and partially hepatectomized rats, respectively) was sufficient to account for the higher level of this protein 3 days after surgery in the latter group.


1966 ◽  
Vol 101 (3) ◽  
pp. 591-597 ◽  
Author(s):  
R M O'Neal ◽  
R E Koeppe ◽  
E I Williams

1. Free glutamic acid, aspartic acid, glutamic acid from glutamine and, in some instances, the glutamic acid from glutathione and the aspartic acid from N-acetyl-aspartic acid were isolated from the brains of sheep and assayed for radioactivity after intravenous injection of [2-(14)C]glucose, [1-(14)C]acetate, [1-(14)C]butyrate or [2-(14)C]propionate. These brain components were also isolated and analysed from rats that had been given [2-(14)C]propionate. The results indicate that, as in rat brain, glucose is by far the best precursor of the free amino acids of sheep brain. 2. Degradation of the glutamate of brain yielded labelling patterns consistent with the proposal that the major route of pyruvate metabolism in brain is via acetyl-CoA, and that the short-chain fatty acids enter the brain without prior metabolism by other tissue and are metabolized in brain via the tricarboxylic acid cycle. 3. When labelled glucose was used as a precursor, glutamate always had a higher specific activity than glutamine; when labelled fatty acids were used, the reverse was true. These findings add support and complexity to the concept of the metabolic; compartmentation' of the free amino acids of brain. 4. The results from experiments with labelled propionate strongly suggest that brain metabolizes propionate via succinate and that this metabolic route may be a limited but important source of dicarboxylic acids in the brain.


Agronomy ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 1637
Author(s):  
Quintino Reis de Araujo ◽  
Guilherme Amorim Homem de Abreu Loureiro ◽  
Cid Edson Mendonça Póvoas ◽  
Douglas Steinmacher ◽  
Stephane Sacramento de Almeida ◽  
...  

Free amino acids in cacao beans are important precursors to the aroma and flavor of chocolate. In this research, we used inferential and explanatory statistical techniques to verify the effect of different edaphic crop conditions on the free amino acid profile of PH-16 dry cacao beans. The decreasing order of free amino acids in PH-16 dry cacao beans is leucine, phenylalanine, glutamic acid, alanine, asparagine, tyrosine, gamma-aminobutyric acid, valine, isoleucine, glutamine, lysine, aspartic acid, serine, tryptophan, threonine, glycine. With the exception of lysine, no other free amino acid showed a significant difference between means of different edaphic conditions under the ANOVA F-test. The hydrophobic free amino acids provided the largest contribution to the explained variance with 58.01% of the first dimension of the principal component analysis. Glutamic acid stands out in the second dimension with 13.09%. Due to the stability of the biochemical profile of free amino acids in this clonal variety, it is recommended that cacao producers consider the genotype as the primary source of variation in the quality of cacao beans and ultimately the chocolate to be produced.


1975 ◽  
Vol 21 (3) ◽  
pp. 414-417 ◽  
Author(s):  
Yasuyuki Doi ◽  
Akikatsu Kataura

Abstract Free amino acids in the tonsils of 20 individuals were measured column chromatographically. Those always found in readily detectable amounts included O-phosphoserine, taurine, O-phosphoethanolamine, aspartic acid, hydroxyproline, threonine, serine, glutamic acid, proline, glycine, alanine, α-amino-n-butyric acid, valine, cystine, methionine, isoleucine, leucine, tyrosine, phenylalanine, ornithine, γ-amino-butyric acid, lysine, histidine, and arginine. Results were compared for three clinical pathological groups and for four age groups. Some abnormal values may result from the pathological conditions.


1956 ◽  
Vol 39 (6) ◽  
pp. 853-868 ◽  
Author(s):  
G. R. Wyatt ◽  
T. C. Loughheed ◽  
S. S. Wyatt

1. Hemolymph was collected for analysis from the silkworm, Bombyx mori, in a series of developmental stages ranging from the second molt to the late pupa. The mean pH of larval hemolymph after collection was found to be 6.45, that of pupal hemolymph, 6.57; in vivo values may be slightly lower. Total dry solids ranged from 5.4 to 10.6 per cent. Total protein ranged from 1.2 to 5.3 per cent, increasing rapidly during the fifth instar. 2. Free amino acids were separated chromatographically and estimated. Of 19 amino acids identified, amounting collectively to 823 to 1497 mg. per 100 ml., glutamine, histidine, and lysine generally occurred in greatest amount. Tryptophan was not detected, and cystine (or cysteine) was found in only one sample. The total free amino acids account for 35 to 55 per cent of the non-protein nitrogen of the plasma. 3. Free sugars, estimated semiquantitatively on chromatograms, comprise glucose, fructose, and sucrose in total amount ranging from about 5 to 40 mg. per 100 ml. Total acid-soluble, ultrafiltrable carbohydrate, estimated as glucose by the anthrone reaction, ranged from 166 to 635 mg. per 100 ml., indicating the presence of low molecular weight sugar derivatives. 4. Inorganic phosphate amounted to 5 to 15 mg. per 100 ml., and acid-soluble organic phosphate to 100 to 200 mg. per 100 ml. The latter fraction includes several substances, of which one was tentatively identified as glucose-6-phosphate and the remainder are as yet unidentified. 5. Single samples of hemolymph were also taken from larvae of the wax moth, Galleria mellonella, and the spruce sawfly, Diprion hercyniae. These contained even higher concentrations of solutes than the silkworm samples, but with a generally similar distribution. The proportions of the free amino acids were different in each species.


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