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

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.

1971 ◽  
Vol 54 (1) ◽  
pp. 61-65
Author(s):  
Arthur Russell Johnson ◽  
Richard L Corliss ◽  
Enrique Fernandez-Flores

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.


1971 ◽  
Vol 41 (1) ◽  
pp. 23-33 ◽  
Author(s):  
A. M. Asatoor ◽  
M. R. Crouchman ◽  
A. R. Harrison ◽  
F. W. Light ◽  
L. W. Loughridge ◽  
...  

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.


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 ◽  
...  

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.


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.


2021 ◽  
Vol 233 ◽  
pp. 02040
Author(s):  
Xuting Bai ◽  
Tao Li ◽  
Honglei Zhao ◽  
Xuepeng Li ◽  
Wenhui Zhu ◽  
...  

Protamex was selected to prepare the hydrolysate. E-tongue, free amino acid combined with soluble peptide analysis were used to detect the flavor changes of Aloididae aloidi during enzymolysis. Degree of proteolysis increased with the prolongation of enzymolysis time, and reached the maximum value at 8 hours. The content of soluble peptide of hydrolysate increased firstly and then decreased in the later process. The E-tongue could effectively distinguish the taste difference of hydrolysates at different enzymolysis time, and the hydrolysate presented strong bitterness and astringency during the whole enzymolysis. The total amount of free amino acids in the hydrolysate increased gradually, and some sweet, umami and bitter amino acids increased in varying degrees during the process of enzymolysis.


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.


1969 ◽  
Vol 50 (2) ◽  
pp. 319-326
Author(s):  
R. R. HARRIS

1. Non-protein and protein nitrogen fractions of the isopod Sphaeroma rugicauda were measured in animals adapted to 100 and 2% sea water. 2. The non-protein nitrogen component was reduced in animals acclimatized to the lower salinity. 3. Free amino acids accounted for 88 and 74% respectively of the non-protein nitrogen in the two salinities. 4. In 2% sea water taurine, proline, glycine, alanine and glutamic acid showed the greatest decreases in concentration compared to the levels measured in animals adapted to 100% sea water. 5. The decrease in total free amino acids of animals acclimatized to 100% sea water and transferred to 2% sea water was measured. 6. The total free amino acid concentration is reduced to the 2% sea water level within 12 hr. after transfer. 7. Free amino acid, haemolymph sodium and total body sodium levels after transfer to 2% sea water were compared. 8. The asymmetry between the fall in haemolymph sodium concentration and the decrease in total body sodium under these conditions is thought to be due to a water shift from the haemolymph into the tissues. 9. It is suggested that the osmotic pressure of the cells falls at a slower rate than that of the haemolymph.


1997 ◽  
Vol 272 (3) ◽  
pp. R991-R994 ◽  
Author(s):  
R. Stancampiano ◽  
F. Melis ◽  
L. Sarais ◽  
S. Cocco ◽  
C. Cugusi ◽  
...  

The effect of oral administration of a tryptophan-free amino acid mixture or the same mixture containing tryptophan (Trp) on hippocampal serotonin (5-HT) extracellular levels was studied using in vivo brain microdialysis of freely moving rats. During chloral hydrate anesthesia rats were implanted with dialysis probes in the dorsal hippocampus, and experiments were performed 24 h later. In vehicle-treated rats, the extracellular levels of 5-hydroxyindolacetic acid (5-HIAA) and 5-HT did not change during 240 min after ingestion. Oral administration of the Trp-free amino acid mixture significantly decreased basal 5-HT and 5-HIAA output 100 min after ingestion (65 and 81% of basal value, respectively) and remained at this level for another 140 min. The amino acid mixture containing Trp failed to significantly change basal extracellular levels of 5-HT, but enhanced that of 5-HIAA by approximately 134%. Moreover, in rats receiving the Trp-free amino acid mixture, the increase of hippocampal 5-HT release induced by d-fenfluramine (206%) was smaller than that released by the same drug in rats receiving the nutritionally balanced amino acid mixture (271%). Thus these results show that removal of Trp from the balanced amino acid mixture decreases spontaneous and d-fenfluramine-induced release of 5-HT in the hippocampus. In conclusion, our study supports the hypothesis that the mood-lowering effect observed in man after ingestion of a Trp-free amino acid mixture is associated with diminished 5-HT release in the brain.


1956 ◽  
Vol 9 (4) ◽  
pp. 539 ◽  
Author(s):  
JV Possingham

The lovel and the qllHnj~itat,jve compositien of the free amino acid fraction of tomato plants grown in full nutrient and in cultures doficiollt ill zinc, copper, nlallganeso, iron. and molybdenum have beon cletormiuecl. 'I'he methods used in the investigation inelude the quantitative estimation of amino aeids by a technique involving paper chromatogl'l1phy, and the cultm'o of tomato plants in highly purified n utriollt solutions.


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