Protein value and amino-acid balance of condensed herring solubles and spontaneously heated herring meal. Chick experiments

1958 ◽  
Vol 51 (2) ◽  
pp. 164-176 ◽  
Author(s):  
B. Laksesvela
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Meal Protein ◽  
Amino Acid Balance ◽  
Microbiological Assays

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.

Liver extract and its free amino acids equally stimulate gastric acid secretion

1980 ◽  
Vol 239 (6) ◽  
pp. G493-G496 ◽  
Author(s):  
E. J. Feldman ◽  
M. I. Grossman
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Secretion ◽  
Gastric Acid Secretion ◽  
Free Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Liver Extract ◽  
Amino Acid Mixture ◽  
Acid Mixture

Using intragastric titration in dogs with gastric fistulas, dose-response studies were carried out with liver extract and with a mixture of amino acids that matched the free amino acids found in liver extract. All solutions were adjusted to pH 7.0 and osmolality to 290 mosmol x kg-1. Doses are expressed as the sum of the concentrations of all free amino acids. At each dose studied (free amino acid concentration: 2.8, 5.6, 11, 23, and 45 mM), acid secretion in response to the free amino acid mixture was not significantly different from that of liver extract. The peak response to both liver extract and the free amino acid mixture occurred with the 23-mM dose and represented about 60% of the maximal response to histamine. The serum concentrations of gastrin after liver extract and the amino acid mixture were not significantly different. It is concluded that in dogs with gastric fistula, gastric acid secretion and release of gastrin were not significantly different in response to liver extract and to a mixture of amino acids that simulated the free amino acid content of liver extract.

Chromatographic Separation of Free Amino Acids in Table Sirups

1971 ◽  
Vol 54 (1) ◽  
pp. 61-65
Author(s):  
Arthur Russell Johnson ◽  
Richard L Corliss ◽  
Enrique Fernandez-Flores
Keyword(s):  
Amino Acids ◽  
Quantitative Analysis ◽  
Amino Acid ◽  
Ion Exchange ◽  
Free Amino Acids ◽  
Free Amino ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Butyl Esters ◽  
Tlc Analysis

Abstract Qualitative chromatographic methods for the separation of free amino acids in table sirups are presented to aid in the development of chemical indices of composition which may be useful in establishing the identity of sirups and detecting their adulteration. Free amino acids in 2 table sirups were isolated on ion exchange columns and eluted with dilute ammonia. The concentrated amino acid mixture in the eluate was spotted directly on silica gel G plates for TLC analysis, or the amino acids were converted to their N-trifluoroacetyl n-butyl esters for GLC analysis. As many as 16 amino acids were qualitatively separated and identified and a potential for quantitative analysis was demonstrated.

scholarly journals Splanchnic-bed transfers of amino acids in sheep blood and plasma, as monitored through use of a multiple U-13C-labelled amino acid mixture

1996 ◽  
Vol 75 (2) ◽  
pp. 217-235 ◽  
Author(s):  
G. E. Lobley ◽  
A. Connell ◽  
D. K. Revell ◽  
B. J. Bequette ◽  
D. S. Brown ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Gas Chromatography Mass Spectrometry ◽  
Acid Mixture ◽  
Body Protein ◽  
Hydrolysis Of

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.

Effect of Glycylglycine on Absorption from Human Jejunum of an Amino Acid Mixture Simulating Casein and a Partial Enzymic Hydrolysate of Casein Containing Small Peptides

1977 ◽  
Vol 53 (1) ◽  
pp. 27-33
Author(s):  
P. D. Fairclough ◽  
D. B. A. Silk ◽  
M. L. Clark ◽  
D. M. Matthews ◽  
T. C. Marrs ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Acid Uptake ◽  
Amino Acid Residues ◽  
Small Peptides

1. A jejunal perfusion technique has been used in normal volunteer subjects to study jejunal absorption of amino acid residues from a partial enzymic hydrolysate of casein in which about 50% of the amino acids existed as small peptides, and also from an equivalent mixture of free amino acids. 2. The effect of a high concentration of the dipeptide glycylglycine on the absorption of amino acid residues from these preparations was studied to quantify the importance of mucosal uptake of intact peptides during absorption of the partial hydrolysate of casein. 3. The results were unexpected. Glycylglycine significantly inhibited absorption of several amino acid residues (aspartic acid + asparagine, serine, glutamic acid + glutamine, proline, alanine, phenylalanine, threonine and isoleucine) from the free amino acid mixture, whereas it significantly inhibited the absorption of only two (serine, glutamic acid + glutamine) from the peptide-containing partial casein hydrolysate. 4. The effect of glycylglycine on absorption of amino acids from the mixture of free amino acids was apparently due to inhibition of amino acid uptake by free glycine liberated from the dipeptide during perfusion. The reason for the failure of glycylglycine to cause extensive inhibition of absorption from the partial hydrolysate is not clear. It may be due to glycylglycine being only a weak inhibitor of peptide uptake, but the possibility that some peptides are taken up by a system unavailable to glycylglycine has to be considered.

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
Keyword(s):  
Amino Acids ◽  
Peritoneal Dialysis ◽  
Amino Acid ◽  
Muscle Tissue ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
Chronic Uraemia ◽  
Muscle Water ◽  
Intracellular Concentrations

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.

Effects on wool growth of the infusion of mixtures of amino acids into the abomasum of sheep

1978 ◽  
Vol 90 (1) ◽  
pp. 173-183 ◽  
Author(s):  
P. J. Reis ◽  
D. A. Tunks
Keyword(s):  
Amino Acids ◽  
Growth Rate ◽  
Amino Acid ◽  
Volume Growth ◽  
Fibre Diameter ◽  
Essential Amino Acids ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Standard Mixture ◽  
Wool Growth

SUMMARYMerino sheep were given abomasal infusions of either mixtures of amino acids or protein during periods of 8 or 12 days. Effects on wool growth were measured using autoradiography and a clipping procedure which allowed time for the emergence of the wool fibres. Estimates of volume growth rate, from the autoradiographic measurements, and of mass of wool grown, from clipping, were in good agreement.An infusion of a standard mixture of 13 amino acids, which included ten essential amino acids in approximately the proportions in casein, consistently stimulated wool growth. The mean increases in volume and mass of wool grown, during 30 infusions, were 66 and 67% respectively. A mixture of ten essential amino acids alone appeared to be as effective as the standard mixture for stimulating wool growth, and there were no significant differences between the effects on wool growth of casein and the standard mixture of amino acids.The omission of methionine from an infusion of the standard mixture of amino acids, or from a mixture of essential amino acids only, inhibited wool growth rate; both fibre diameter and length of wool grown per day were reduced to below the control values. In addition, the strength of the fibres was considerably reduced.Infusions of zein and of an amino acid mixture simulating the essential amino acid composition of zein both inhibited wool growth rate, due to a reduction in fibre diameter. Similar effects on wool growth were observed when any one of three essential amino acids (lysine, isoleucine or leucine) was omitted from an infusion of the standard mixture of amino acids. The omission of five other essential amino acids (arginine, histidine, phenylalanine, threonine or valine) from the infusion, or variations in the proportions of leucine, lysine or methionine, had no appreciable effects on wool growth.

Intestinal Absorption of Oligopeptides in Cystinuria

1971 ◽  
Vol 41 (1) ◽  
pp. 23-33 ◽  
Author(s):  
A. M. Asatoor ◽  
M. R. Crouchman ◽  
A. R. Harrison ◽  
F. W. Light ◽  
L. W. Loughridge ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino ◽  
Intestinal Transport ◽  
Tolerance Test ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Test Technique ◽  
Rat Gut

1. The intestinal transport of oligopeptides containing either lysine or arginine has been compared with that of the corresponding free amino acids in six homozygous cystinuric patients and in six normal adult subjects by use of the oral tolerance test technique. 2. No difference was found in the absorption of lysine from l-lysylglycine and an equivalent mixture of free lysine and glycine. 3. In comparisons of serum increments of lysine and arginine after oral casein and an equivalent free amino acid mixture there was no difference in the case of lysine but rise of serum arginine was higher in three cystinuric patients after the whole protein than after the amino acids. 4. Studies of urinary piperidine and pyrrolidine output in a single cystinuric patient supported the results of the tolerance tests. 5. Absorption rates of the dipeptides l-lysylglycine and l-arginyl-l-aspartate from an isolated loop of rat gut are compared with those of an equivalent free amino acid mixture. No difference was found for the former peptide, but in the latter absorption rates of arginine were higher after the amino acid mixture.

scholarly journals Effect of leucine on intestinal absorption of tryptophan in rats

1985 ◽  
Vol 54 (3) ◽  
pp. 695-703 ◽  
Author(s):  
Chisae Umezawa ◽  
Yuko Maeda ◽  
Kanji Haba ◽  
Mariko Shin ◽  
Keiji Sano
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Intestinal Absorption ◽  
Digestive Tract ◽  
Causal Relation ◽  
Control Diet ◽  
Essential Amino Acids ◽  
Amino Acid Mixture ◽  
Side Chain ◽  
Acid Mixture

1. To elucidate the causal relation between leucine and the lowering of hepatic NAD content of rats fed on a leucine-excessive diet (Yamada et al. 1979), the effect of leucine on intestinal absorption of tryptophan was investigated.2. Co-administration of [3H]tryptophan and leucine, with leucine at ten times the level of tryptophan, delayed absorption of L-[side chain 2,3-3H]tryptophan from the digestive tract and incorporation of [3H]tryptophan into portal blood, the liver and a protein fraction of the liver. After 120 min, more than 95% of tryptophan was absorbed whether [3H]tryptophan was administered with or without leucine.3. Co-administration of a mixture of ten essential amino acids, in proportions simulating casein, with [3H]tryptophan markedly delayed absorption of tryptophan from the digestive tract. The addition of supplementary leucine to the amino acid mixture, however, caused no further delay.4. In rats prefed a leucine-excessive diet for 1 week [3H]tryptophan was absorbed at the same rate as in rats fed on a control diet.5. The results indicate that competition between tryptophan and leucine for intestinal absorption did not cause lowering of hepatic NAD.

scholarly journals The effects of maternal protein restriction on the growth of the rat fetus and its amino acid supply

1999 ◽  
Vol 81 (3) ◽  
pp. 243-250 ◽  
Author(s):  
William D. Rees ◽  
Susan M. Hay ◽  
Viv Buchan ◽  
Christos Antipatis ◽  
Robert M. Palmer
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
G Protein ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
Maternal Serum ◽  
Rat Fetus ◽  
Adult Disease ◽  
Low Protein

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.

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