Intracellular Free Amino Acids in Muscle Tissue of Patients with Chronic Uraemia: Effect of Peritoneal Dialysis and Infusion of Essential Amino Acids

1978 ◽  
Vol 54 (1) ◽  
pp. 51-60 ◽  
Author(s):  
J. Bergström ◽  
P. Fürst ◽  
L.-O. Norée ◽  
E. Vinnars

1. Free amino acids were determined in the plasma and in the muscle tissue of 14 patients with chronic uraemia; eight were not on dialysis and six were having regular peritoneal dialysis. The concentration of each amino acid in muscle water was calculated with the chloride method. 2. In both groups of patients there were low intracellular concentrations of threonine, valine, tyrosine and carnosine, and high glycine/valine and phenylalanine/tyrosine ratios. Both groups of patients had increased amounts of 1- and 3-methylhistidine in plasma and in muscle water. 3. The non-dialysed patients had low intracellular concentrations of lysine, and the dialysed patients had high intracellular concentrations of lysine, isoleucine, leucine and of some of the non-essential amino acids. 4. After peritoneal dialysis for 22 h, the plasma concentration of several amino acids decreased but the intracellular concentrations of most amino acids did not change significantly. 5. Intravenous administration of essential amino acids and histidine during the last 4 h of dialysis increased in muscle the total free amino acids, the ratio of essential to non-essential amino acids and the valine and phenylalanine concentrations. 6. The results demonstrated that the plasma and muscle concentrations of several amino acids are grossly abnormal in chronic uraemia. Non-dialysed and dialysed patients exhibit important differences, especially in the intracellular amino acid patterns. Infusion of essential amino acids may result in enhancement of protein synthesis.

1996 ◽  
Vol 75 (2) ◽  
pp. 217-235 ◽  
Author(s):  
G. E. Lobley ◽  
A. Connell ◽  
D. K. Revell ◽  
B. J. Bequette ◽  
D. S. Brown ◽  
...  

AbstractThe response in whole-body and splanchnic tissue mass and isotope amino acid transfers in both plasma and blood has been studied in sheep offered 800 g lucerne (Medicago sutiva) pellets/d. Amino acid mass transfers were quantified over a 4 h period,by arterio-venous procedures, across the portal-drained viscera (PDV) and liver on day 5 of an intravenous infusion of either vehicle or the methylated products, choline (0.5 g/d) plus creatine (10 g/d). Isotopic movements were monitored over the same period during a 10 h infusion of a mixture of U-13C-labelled amino acids obtained from hydrolysis of labelled algal cells. Sixteen amino acids were monitored by gas chromatography-mass spectrometry, with thirteen of these analysed within a single chromatographic analysis. Except for methionine, which is discussed in a previous paper, no significant effects of choline plus creatine infusion were observed on any of the variables reported. Whole-body protein irreversible-loss rates ranged from 158 to 245 g/d for the essential amino acids, based on the relative enrichments (dilution of the U-13C molecules by those unlabelled) of free amino acids in arterial plasma, and 206-519 g/d, when blood free amino acid relative enrichments were used for the calculations. Closer agreement was obtained between lysine, threonine, phenylalanine and the branched-chain amino acids. Plasma relative enrichments always exceeded those in blood (P < 0.001), possibly due to hydrolysis of peptides or degradation of protein within the erythrocyte or slow equilibration between plasma and the erythrocyte. Net absorbed amino acids across the PDV were carried predominantly in the plasma. Little evidence was obtained of any major and general involvement of the erythrocytes in the transport of free amino acids from the liver. Net isotope movements also supported these findings. Estimates of protein synthesis rates across the PDV tissues from [U-13C] leucine kinetics showed good agreement with previous values obtained with single-labelled leucine. Variable rates were obtained between the essential amino acids, probably due to different intracellular dilutions. Isotope dilution across the liver was small and could be attributed predominantly to uni-directional transfer from extracellular sources into the hepatocytes and this probably dominates the turnover of the intracellular hepatic amino acid pools.


1999 ◽  
Vol 81 (3) ◽  
pp. 243-250 ◽  
Author(s):  
William D. Rees ◽  
Susan M. Hay ◽  
Viv Buchan ◽  
Christos Antipatis ◽  
Robert M. Palmer

Maternal protein deficiency causes fetal growth retardation which has been associated with the programming of adult disease. The growth of the rat fetus was examined when the mothers were fed on diets containing 180, 90 and 60 g protein/kg. The numbers of fetuses were similar in animals fed on the 180 and 90 g protein/kg diets but the number was significantly reduced in the animals fed on the 60 g protein/kg diet. The fetuses carried by the mothers fed on the 90 g protein/kg diet were 7·5% heavier than those of mothers fed on 180 g protein/kg diet on day 19 of gestation, but by day 21 the situation was reversed and the fetuses in the protein-deficient mothers were 14% smaller. Analysis of the free amino acids in the maternal serum showed that on day 19 the diets containing 90 and 60 g protein/kg led to threonine concentrations that were reduced to 46 and 20% of those found in animals fed on the control (180 g/kg) diet. The other essential amino acids were unchanged, except for a small decrease in the branched-chain amino acids in animals fed on the 60 g protein/kg diet. Both low-protein diets significantly increased the concentrations of glutamic acid+glutamine and glycine in the maternal serum. On day 21 the maternal serum threonine levels were still reduced by about one third in the group fed on the 90 g protein/kg diet. Dietary protein content had no effect on serum threonine concentrations in non-pregnant animals. Analysis of the total free amino acids in the fetuses on day 19 showed that feeding the mother on a low-protein diet did not change amino acid concentrations apart from a decrease in threonine concentrations to 45 and 26% of the control values at 90 and 60 g protein/kg respectively. The results suggest that threonine is of particular importance to the protein-deficient mother and her fetuses. Possible mechanisms for the decrease in free threonine in both mother and fetuses and the consequences of the change in amino acid metabolism are discussed.


1983 ◽  
Vol 50 (2) ◽  
pp. 383-390 ◽  
Author(s):  
Kyu-Il Kim ◽  
Henry S. Bayley

1. Piglets were weaned at 3 d of age and were introduced to liquid diets in which 400 g/kg protein was supplied as skim-milk powder and the balance as a mixture of free amino acids. The skim milk contributed 2·3 g methionine and 1·4 g cystine/kg diet; the experimental diets were made by supplementing these levels with free amino acids.2. The adequacy of the test level of the amino acid in the diet was assessed by measuring the oxidation of [1−14]phenylalanine as an indicator of the partition of the essential amino acids between incorporation into protein and degradation. Radioactivity recovered as carbon dioxide was used as a measure of catabolism.3. Addition of 0·2, 0·4, 0·7, 1·2 and 1·7 g L-methione/kg to a diet containing 5 g cystine and 3 g choline chloride/kg showed that phenylalanine catabolism was minimal for the diet with 2·7 g methionine/kg indicating that this is the dietary requirement for methionine to serve as a source of methionine residues for protein synthesis.4. Addition of D-methionine to produce a series of diets with graded levels of methionine showed that the D-isomer was less effective than the L-isomer in reducing phenylalanine catabolism: the addition of 0·8 g D-methionine/kg diet was needed to produce the same effect as 0·4 g L-methionine/kg diet showing that the replacement value of D-methionine for L-methionine was 50% in the young pig.5. To investigate the influence of cystine on methionine requirement, diets with varying levels of methionine and cystine were prepared. Oxidation of [U-14C]methionine was used as an indication of an excess of methionine, and the results showed that increasing the dietary methionine level above 3·0 g/kg in diets containing 1·4 g cystine/kg provided an excess of methionine for oxidation. This indicated a sulphur amino acid requirement of 4·4 g/kg, one-third of this being supplied as cystine.


1970 ◽  
Vol 24 (4) ◽  
pp. 1071-1081 ◽  
Author(s):  
T. G. Taylor ◽  
J. J. Waring ◽  
R. K. Scougall

1. The changes occurring in the free amino acids of the plasma of laying hens in relation to egg formation have been investigated in fed and starved hens in three experiments, each with eight birds.2. The mean concentrations of most amino acids and of the totals were higher at night than in the morning.3. In general, egg formation was associated with increases in the concentrations of non- essential and decreases in the concentrations of essential amino acids. Cystine and glutamic acid tended to behave like the essential amino acids.4. After 40 h starvation seven amino acids, particularly serine, histidine and lysine, in- creased in concentration and only three, proline, ornithine and arginine, decreased significantly.5. When eight cocks were injected with oestrogen most of the amino acids increased in con-centration. The essential amino acids (with the exception of phenylalanine), serine, proline, cystine and ornithine showed the greatest increases.6. The results are discussed in relation to the possibility that the voluntary food intake of hens may be influenced by changes in the plasma levels of one or more essential amino acids associated with the synthesis of egg albumen. Arginine appeared to be the only amino acid that might possibly fulfil this role.7. It was concluded that investigations of changes in the free amino acids of hen plasma are unlikely to provide a useful approach to a study of the amino acid requirements or the nutritive value of particular proteins for egg production.


Author(s):  
L. V. Vronska ◽  
A. Ye. Demyd

The aim of the research was to study the amino acid profile of the phaseolus vulgaris pods and extract prepared of them. Materials and methods. Five samples of raw material of phaseolus vulgaris pods (erect herbaceous bushes varieties with white seeds) were collected in the Ternopil and Volyn regions, dry extract of phaseolus vulgaris pods was obtained according to previously developed technology. The study of amino acid composition of the raw materials of phaseolus vulgaris pods and extract prepared of them was carried out using a thin-layer chromatography (TLC) and a high-performance liquid chromatography (HPLC). Results and discussion. The better separation of amino acids in TLC-research of the raw material of phaseolus vulgaris pods was observed in the system of solvents isopropanol - formic acid - water (40: 2: 10). As a result of the study, aspartic and glutamic acids, glycine, valine, tyrosine and leucine were identified. The amino acid profile of the studied samples of raw material is quite homogeneous in composition: 7 essential amino acids (histidine, threonine, valine, methionine, phenylalanine, isoleucine and leucine) and 8 non-essential amino acids (aspartic and glutamic acids, arginine, serine, glycine, alanine, tyrosine and proline); lysine was found among the bound amino acids in the 4th sample of raw material. Proline predominates in all samples of raw materials among free amino acids. Among the bound amino acids the content of glutamic acid, which is the product of the glutamine hydrolysis, is the highest. The content of glycine, serine and alanine is also high. Among the essential amino acids, leucine, phenylalanine, histidine, threonine, isoleucine, valine were determined in content descending order. The quantitative determination of amino acids in the extract of phaseolus vulgaris pods proved that the content of proline was the highest (12.47 mg / g); the content of some compounds was also high: aspartic (5.41 mg / g) and glutamic (3.41 mg / g) acids, arginine (5.10 mg / g; both in free and bound forms), glycine (1.02 mg / g) and serine (1.04 mg / g). Among the essential amino acids in the extract, the amount of valine (0.80 mg / g), phenylalanine (0.67 mg / g), threonine (0.66 mg / g), leucine (0.63 mg / g) and isoleucine (0.58 mg / g) was a little different. The total content of amino acids in the extract was 3.2%. Conclusions. 1. The amino acid profile of five samples of phaseolus vulgaris pods was studied by the HPLC method. It has been established that the composition is quite homogeneous, and the total content varies within 0.7-1.1%. 2. In the dry extract of phaseolus vulgaris pods the content of 5 essential and 7 non-essential amino acids has been determined. The content of free amino acids in the extract is 0.52%; the total content of free and bound amino acids is 3.2%. 3. When studying the stability and establishing the shelf life of the dry extract of phaseolus vulgaris pods, it is necessary to take into account the presence of free amino acids and protein substances.  


1990 ◽  
Vol 79 (4) ◽  
pp. 331-337 ◽  
Author(s):  
J. Bergström ◽  
P. Fürst ◽  
E. Vinnars

1. The effect of a protein-free meal and a protein-rich meal on the concentration of free amino acids in plasma and muscle tissue was studied in eight healthy subjects. The energy content of the protein-free meal was 3800 kJ. The protein-rich meal was identical in composition except that 50 g of bovine serum albumin was added. Plasma and samples from the quadriceps femoris muscle (percutaneous muscle biopsy) for amino acid determination were collection before and at 1, 3, 5 and 7 h after the meal. 2. After the protein-free meal the concentrations of most essential amino acids and of some non-essential amino acids in plasma decreased continuously below basal levels at 5–7 h. The muscle concentration of essential amino acids fell too, reaching its nadir 3–5 h after the meal. The decrease in plasma amino acid concentration was smaller than the decrease in muscle concentration for all essential amino acids except phenylalanine. 3. The concentrations of most amino acids in plasma increased transiently 1 and 3 h after the protein-rich meal; histidine and several non-essential amino acids fell below the basal levels at 5–7 h after the meal. In muscle, threonine, valine, leucine, lysine and alanine were increased at 1 and 3 h after the protein-rich meal; isoleucine, serine and glycine fell below the basal level after 5 and 7 h. For the essential amino acids except threonine and lysine, the increase in plasma concentration was greater than the increase in muscle concentration. 4. Correlations were observed between the relative content of the essential amino acids in the bovine serum albumin and the increase in concentration of these amino acids in plasma and muscle. Methionine and isoleucine, which had the lowest content in bovine serum albumin, fell below basal levels in plasma and (for isoleucine) in muscle 5–7 h after the meal, suggesting that these two amino acids might have been limiting for protein synthesis. 5. Amino acid analysis in plasma and muscle samples taken postprandially should be evaluated with caution considering the strong influence of meal composition on plasma and muscle free amino acid profiles.


1958 ◽  
Vol 51 (2) ◽  
pp. 164-176 ◽  
Author(s):  
B. Laksesvela

1. In a series of tests chicks were fed up to 4 weeks of age on a ‘purified’ diet supplemented with 10% of protein from either herring meal or condensed herring solubles.2. The solubles alone appeared of negligible value as a protein source, but certain mixtures of solubles and meal protein proved superior to meal alone, although the levels of the essential amino acids plus cystine and tyrosine were lower in the mixture than in meal alone. The supplementary effect may possibly be due to changes in the aminoacid ratio or balance.3. Only tryptophan improved growth and viability when free amino acids were added singly to the solubles. Simultaneous supply of all 10 essential amino acids elevated growth to about 80% of that on meal alone. A combination of tryptophan, isoleucine, histidine and phenylalanine appeared nearly as effective as the 10. Depressant effects of free amino acids at the low levels used were also met with. The chick results followed closely the predictions made from the results of microbiological assays of the amino-acid composition of the solubles, and these were in conformity with the composition of the ‘ideal’ amino-acid mixture for chicks proposed by Fisher & Johnson (1957).4. The small weight gains of the chicks on solubles alone consisted largely of water rather than true tissue. Appetite appeared to be governed by the balance of amino acids, this appearing to be more important than the absolute levels fed. This applied to diets with heated meal as well as the solubles.


1973 ◽  
Vol 28 (7-8) ◽  
pp. 449-451 ◽  
Author(s):  
G. Peter ◽  
H. Angst ◽  
U. Koch

Free and protein-bound amino acids in serum and scales were investigated. In serum the bound amino acids of psoriatics are significantly higher with exception of Pro, Met, Tyr and Phe in contrast to normal subjects. For free amino acids the differences between normal subjects and psoriatics found in serum and scales are not significant. Results are discussed in relation to the single amino acids and the biochemical correlations are outlined which takes the pathological process as a basis.


PEDIATRICS ◽  
1984 ◽  
Vol 73 (6) ◽  
pp. 879-879
Author(s):  
T. A. TEDESCO ◽  
S. A. BENFORD ◽  
R. C. FOSTER ◽  
L. A. BARNESS

To the Editor.— Currently accepted dietary management of citrullinemia and other urea cycle disorders includes protein restriction, sodium benzoate, and dietary supplements of keto acids or essential amino acids with postblock intermediates such as arginine in citrullinemia and arginino-succinic aciduria. When a child survives the neonatal period on such a regimen and solid foods are introduced into the diet, there is at least one fruit that should be avoided, Citrullus Vulgaris, commonly known as watermelon. Quantitation of free amino acids extracted from 1 g wet weight of watermelon fruit yielded the following (in mmoles per gram wet weight): Phenylalanine, 1.25; histidine, 0.24; tryptophan, 0.35; lysine, 0.82; ornithine, 0.32; arginine, 11.36; aspartic acid, 0.97; threonine, 0.74; serine, 1.05; glutamine, 3.86; glutamic acid, 1.38; citrulline, 23.68; alanine, 1.15; valine, 0.17; isoleucine, 1.24; leucine, 0.24.


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