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PubMed1980

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

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.

Amino Acids↗
PubMed1983

Determination of amino acid requirements of young pigs using an indicator amino acid.

Mixtures of skim milk and free amino acids were compared as diets for pigs which would allow manipulation of dietary amino acid levels. Piglets gained 208 g/d between 3 and 14 d of age on the skim-milk diet, but replacement of 600 g/kg of the dietary nitrogen with free amino acids reduced growth rate to 148 g/d. Supplementation of a lysine-deficient diet with lysine reduced the catabolism of [14C]phenylalanine showing that phenylalanine catabolism could be used as an indicator of the adequacy of diet with respect to another essential amino acid. The dietary level of phenylalanine which would provide an excess for catabolism by the piglet was estimated directly by measuring the influence of dietary phenylalanine level on [14C]phenylalanine oxidation. Reduction of the dietary phenylalanine level below 7 g/kg had no effect on phenylalanine oxidation, whereas increasing the dietary phenylalanine level above 7 g/kg resulted in a linear increase in phenylalanine oxidation. An indirect estimate of histidine requirement was made by examining the influence of dietary histidine level on [14C]phenylalanine oxidation. In diets containing more than 4 g histidine/kg, phenylalanine oxidation was minimal. In diets containing less than 4 g histidine/kg, [14C]phenylalanine oxidation increased as the level of dietary histidine was reduced. This showed that the utilization of the essential amino acid phenylalanine, for protein synthesis, was not limited by histidine supply in diets containing more than 4 g histidine/kg. A direct estimate of histidine requirement was made by examining the influence of dietary histidine level on [14C]histidine oxidation. Diets with more than 4 g histidine/kg contained an excess which was catabolized: there was a linear increase in histidine oxidation in response to dietary histidine levels greater than 4 g/kg. This confirmed the previous indirect estimate of histidine requirement.

Amino Acids↗
PubMed1984

Treatment of dietary casein with formaldehyde reduces its hypercholesterolemic effect in rabbits.

Rabbits were fed cholesterol-free, semipurified diets containing 42% (wt/wt) casein or 21% casein plus one of the following nitrogen sources: soy isolate, amino acid mixture simulating casein, amino acid mixture simulating soy isolate, formaldehyde-treated casein or formaldehyde-treated soy isolate. Two additional groups of rabbits were fed the 42% casein diet and the diet containing casein plus soy isolate to which 0.4% (wt/wt) pure formaldehyde was added, this amount being identical to the amount of formaldehyde present in the diets with formaldehyde-treated proteins. Growth was somewhat reduced on the three diets containing 42% casein. The diet containing 42% casein to which no formaldehyde had been added induced severe hypercholesterolemia, the level of serum cholesterol after 8 weeks being about 10 mmol/L. The hypercholesterolemia was markedly reduced by the replacement of half of the casein by soy isolate, formaldehyde-treated soy isolate or formaldehyde-treated casein. No significant reduction of the concentration of serum cholesterol was seen when half of the 42% casein was replaced by an amino acid mixture imitating either casein or soy isolate. Formaldehyde per se did not significantly influence the level of serum cholesterol. We conclude that the differential tertiary structure of intact casein and soy isolate is an important factor in determining the cholesterolemic responses in rabbits to these proteins.

Animals↗
PubMed1982

Vagal unitary responses to intestinal amino acid infusions in the anesthetized cat: a putative signal for protein induced satiety.

Single unitary discharges in the nodose ganglia were recorded extracellularly in chloralose anesthetized cats while amino acid solutions were being perfused through the small intestine via implanted cannulae. Test infusions consisted of either amino acid mixtures (12 amino acids; 120 mM in all) or individual amino acids (50 mM each) dissolved in Krebs Henseleit buffer. Units which were activated by amino acid infusions were also tested with 10% glucose infusions performed in the same way. Control infusions consisted of either buffer alone or a physiological saline solution isotonic to the test solution. All perfusions were performed at 38 degrees C, pH 7.4 by means of a syringe over a 10 second period. Out of 1250 vagal units activated by electrical vagal stimulation, 92 units showed an increased firing rate in response to amino acid intestinal perfusions. Of these, only 1/7 were also responsive to glucose perfusions. Osmotic, thermal or mechanical stimuli associated with infusions did not modify vagal responses to the amino acids. Among vagal units responding only to amino acid but not to glucose infusion, some were activated in a specific manner, depending on the specific amino acid infused intraduodenally. These neurons illustrated a very strict specificity regarding the nature of chemical stimuli. The very short latency, mean of 9 sec +/- 0.7 (SE) of these vagal neurons to amino acid infusions unequivocally indicates that chemoreceptors are located at the preabsorptive level. The corresponding fibers were non-myelinated (conduction velocities: 0.8/1.4 m/sec.) and were of the C type. The functional characteristics of these vagal amino acid receptors are discussed in terms of the role of intestinal signals in short term protein satiety.

Animals↗
PubMed1983

Effect of substrate on the regulation of exoprotease production by Pseudomonas aeruginosa ATCC 10145.

Exoprotease production by Pseudomonas aeruginosa ATCC 10145 was growth-associated when cultures were grown on complex substrates such as proteins but it occurred during the decelerating growth phase when the organism was grown on amino acids, mixtures of amino acids or simple carbon sources. NH4Cl and simple carbon sources caused repression. Exoprotease was produced in chemostat cultures in response to growth under any of the nutrient limitations studied (carbon, nitrogen or phosphate). Furthermore, by growing at rates less than approximately 0.1 h-1, the repression of enzyme production could be overcome to a large degree. At low growth rates there was an inverse relationship between growth rate and exoprotease production. Thus, exoprotease production was depressed by available energy sources and was increased in response to any nutrient limitation.

Amino Acids↗
PubMed1976

Nutritional disturbances of protein metabolism in the liver.

Nutritional disturbances of protein metabolism in the liver are reviewed in relation to feeding experimental animals the following diets: a) purified diets deficient in amino acids; b) amino acid mixtures or single amino acids; c) protein-free (amino acid-free) diets; or d) hypertonic or hypotonic solutions. The effects of tube-feeding the diets or dietary components for days, hours, or minutes on hepatic polyribosomes and protein synthesis are described. Force-feeding a purified diet free of single essential amino acids induces within days morphologic changes resembling those that occur in humans with kwashiorkor, a world-wide nutritional deficiency disease in children. In this kwashiorkor-like model, hepatic protein synthesis and polyribosomal aggregation are increased. Administration of a complete amino acid mixture or tryptophan alone, but no other single amino acid, produces a rapid stimulation (within minutes) of hepatic protein synthesis and polyribosomal aggregation in animals that had been fasted, fed, or treated with hepatotoxic agents. A single tube-feeding of a protein-free (amino acid-free) diet induces within hours an increase in hepatic protein synthesis in fasted animals. Administration of hypertonic solutions rapidly (within minutes) inhibits, while administration of hypotonic solutions rapidly increases, hepatic protein systhesis. These experimental findings are reviewed in terms of how alterations in regulatory controls of hepatic protein synthesis may be influenced by nutritional disturbances. Such information may be of importance in designing and utilizing nutritional approaches in the therapy of liver diseases.

Amino Acids, Essential↗
PubMed1975

Nitrogen retention and plasma amino acids of men who consumed isonitrogenous diets containing egg albumen or mixtures of amino acids.

Experimental diets that furnished approximately 6.0 g of nitrogen per day were consumed by young men. Nitrogen retention was not altered significantly when egg albumen was replaced by its constituent essential and nonessential amino acids or by the essential amino acids (including cystine, tyrosine and histidine) plus a source of nonspecific nitrogen. Concentrations of essential amino acids in fasting or postprandial plasma were not influenced significantly by source of amino acids or by replacement of nonessential amino acids by nonspecific nitrogen; but concentrations of certain nonessential amino acids were altered by treatment. Responses to an elemental diet or to a similar diet in which egg albumen replaced the amino acid mixture did not differ significantly.

Adult↗
PubMed1989

Enhanced release of cholecystokinin by dietary amino acids in chicks (Gallus domesticus).

1. The effect of dietary amino acids and protein on cholecystokinin (CCK) release into plasma was investigated in chicks by feeding a meal through a stomach tube, followed by the CCK determination with specific CCK-8 antibody. 2. The results showed that both isolated soya protein and an amino acid mixture simulating the amino acid composition of the soya protein increased the release of CCK, though to a lesser extent with a delayed response in the former, when added to a protein-free diet. 3. Among amino acids added singly to the protein-free diet, phenylalanine was more efficient than arginine and valine, exerting a response almost identical to the complete amino acid mixture.

Amino Acids↗
PubMed1975

The effect of phenformin on amino acid-induced insulin secretion in diabetics.

Twenty-one patients with mild maturity-onset diabetes were given introduodenal infusions of an amino acid mixture (0.5 g amino acids per kg body weight). In 9 other patients L-arginine was infused intravenously in a constant dose of 25 g. Alpha-amino nitrogen, blood glucose and plasma insulin levels were assayed under control conditions and after three days of treatment with phenformin, 150 mg daily, plus the same 150 mg dose 60 min before the second loading. Intraduodenal infusion of the amino acid mixture provoked a greater increase in plasma insulin than intravenous infusion of L-arginine, this increase being significantly inhibited by phenformin only in the first case. Since no evident influence of phenformin on the intestinal absorption of amino acids could be demonstrated, this effect may be explained by a local action on the intestinal wall exposed to high concentrations of the drug, resulting in the inhibition of the insulin secretion stimulating activity of the gut.

Adult↗
PubMedDate not supplied

Parenteral branched-chain amino acid treatment and avian dystrophy.

Genetically homozygous line 413 dystrophic chickens were given twice-daily intraperitoneal injections of solutions containing branched-chain amino acids (BCCA-leucine, valine, isoleucine) either alone or in combination; and their alpha-ketoacid analogs (alpha-ketoisocaproic and alpha-ketoisovaleric acids). Another trial consisted of an amino acid mixture containing BCAA. Amino acid supplementation in each case significantly prolonged righting ability measured regularly by a standardized flip-test procedure. Enhanced functional ability was not generally accompanied by a decrease in plasma creatine kinase activity. However, a measurable increase in the affected pectoralis major muscle mass and protein content (female chickens in particular) was found with BCAA therapy. Moreover, the increase in muscle bulk was attended in some cases by a reduction in the relative number of degenerating fibers quantitated microscopically. Contrariwise, the amino acid mixture caused a reduction in pectoralis muscle mass. It is concluded that parenteral BCAA therapy offers limited benefit in retarding dystrophic symptoms in the chickens.

Amino Acids↗
PubMed1984

Portal absorption of small peptides in rats under unrestrained conditions.

The intestinal absorption of small peptides was investigated in rats under unrestrained conditions. The peptide utilized in the experiment was hydrolysate of egg white protein with an average molecular weight of about 350 and containing less than 10% of free amino acids. We compared the intestinal absorption of these small peptides with that of an amino acid mixture with the same small peptide amino acid composition by determining the concentration of individual amino acids in portal blood after a single administration of a nitrogen source. The absorptive intensity of each amino acid was calculated from its rate of elevation in the portal blood; it was higher in the small peptides. The proportion of the amount of each amino acid absorbed in portal blood from small peptides was much more like the composition of the administered amino acids than like that from the amino acid mixture. Among the amino acids administered in the mixture, some amino acids such as L-tyrosine, L-threonine, L-serine and L-histidine increased more slowly in the blood than others. These results suggested that the small peptide formula was utilized more effectively than the amino acid mixture and had higher nutritive value.

Alanine↗
PubMed1974

The absorption of a mixture of amino acids by rat small intestine.

1. The absorption of a mixture of amino acids by the small intestine has been studied in vitro with mucosal slices from rat jejunum. The mixture contained eighteen amino acids and was used at a concentration of 9.5 mM in the incubation medium. The uptake of fifteen of the amino acids was followed in each sample with the aid of an amino acid analyser.2. The endogenous amino acid content of the slices decreased during preparation and further substantial losses occurred when the slices were preincubated for 30 sec before the addition of the amino acid mixture to the incubation medium.3. When the slices were incubated with the amino acid mixture for 4.5 min all of the amino acid studied were accumulated to give concentration ratios of approximately 2.0.4. The amino acids were taken up rapidly by the tissue so that on average 82% of the amino acids absorbed in 4.5 min had already accumulated after one min of incubation.5. The data for individual amino acids revealed no obvious competition between the various amino acids, and the extent to which the various amino acids were accumulated by the tissue was proportional to their concentrations in the mixture.6. When the Na(+) in the incubation medium was replaced by Li(+), the slices accumulated all of the amino acids studied to concentrations significantly higher than those in the incubation medium. However, the concentration ratios obtained with the Li(+) medium were all lower than those obtained with the Na(+) medium and averaged slightly more than 1.5.7. When the Na(+) in the incubation medium was replaced by K(+) there was little amino acid accumulation, although concentration ratios significantly greater than one were achieved for aspartic acid, glycine, histidine and methionine.

Amino Acids↗
PubMedDate not supplied

Is muscle protein turnover regulated by intracellular glutamine during sepsis?

BACKGROUND: Low muscle glutamine levels during sepsis are associated with reduced protein synthesis and elevated protein breakdown, in particular myofibrillar protein breakdown. It is not known if this is a causal or coincidental relationship. We tested the hypothesis that muscle protein turnover rates are directly regulated by glutamine. METHODS: Paired extensor digitorum longus muscles from nonseptic (sham-operated) and septic rats (16 hours after cecal ligation and puncture) were incubated in the absence or presence of 15 mmol glutamine/L. The effect of glutamine was tested in unsupplemented medium or in medium containing 1 mU/mL of insulin or a mixture of amino acids at normal plasma concentrations. Protein synthesis was measured as incorporation of 14C-phenylalanine into protein; total and myofibrillar protein breakdown was determined by measuring tyrosine and 3-methylhistidine, respectively. RESULTS: Muscles accumulated intracellular glutamine well above normal concentrations in the presence of 15 mmol glutamine/L. In spite of this, protein synthesis was not affected by glutamine, neither when muscles were incubated in unsupplemented medium nor in medium containing insulin or amino acid mixture. Total protein breakdown was not influenced by glutamine when muscles were incubated in unsupplemented medium or with insulin but was reduced by glutamine in the presence of an amino acid mixture. Myofibrillar protein breakdown was unaffected by glutamine in unsupplemented medium and in medium containing insulin but was increased by glutamine in the presence of amino acid mixture. CONCLUSION: Reduced muscle protein synthesis and increased myofibrillar protein breakdown during sepsis are probably not caused by the low intracellular glutamine levels noticed in this condition.

Amino Acids↗
PubMed1969

A comparison of the effects of ultraviolet and ionizing radiations on trypsin activity and on its constituent amino acids.

Photons of 254nm. u.v. light, (60)Co gamma-rays and 1Mev electrons produce different patterns of destruction of individual amino acids in dried films of trypsin and in the corresponding amino acid mixture. For example, in the amino acid mixture u.v. light destroys tyrosine, tryptophan and cystine, whereas in trypsin only cystine is disrupted but with 10 times the initial yield. Further, in the amino acid mixture loss of half-cystine is a simple exponential function of dose, but in trypsin there appear to be two exponential components of the loss with yields that differ by a factor of 35. Both the gamma-rays and electrons destroy half-cystine, tryptophan, histidine and methionine in the amino acid mixture with remarkably high yields, whereas in trypsin doses that destroy almost all of the enzymic activity produce no detectable destruction of amino acid residues. These marked differences between the two preparations show that the radiation-sensitivity of a given amino acid alone and in a protein is different, and suggests that in trypsin there is fairly extensive migration of energy, charge or both with localization of damage at specific sites determined by this enzyme's internal organization. All three types of radiation produce appreciable amounts of ;damaged' (not completely inactivated) molecules which are prevented from reassuming an active configuration by the addition of 5.5m-urea; thiol reagents have a similar effect after bombardment with u.v. light or electrons. The patterns of destruction produced by gamma-rays and by electrons in both the amino acid mixture and in trypsin are different (some of the yields vary by a factor of 30). This result appears to be inconsistent with the popular belief that most of the energy absorbed from gamma-rays is associated with very-high-energy electrons.

Amino Acids↗
PubMed1986

In vitro and clinical studies on intravenous feeding mixtures comprising fat emulsion, amino acid and electrolytes.

This paper describes the effect of the amino acid mixture Freamine II on the physical stability of Intralipid fat emulsion. The amino acid-fat emulsion mixture was also administered to patients requiring intravenous nutrition and its clinical and biochemical effects were assessed. The amino acid-fat emulsion mixture was stable on storage for 48 hours as judged by flocculation and particle growth measurements made in the presence of 20 mmol/1 monovalent cations at 2 mmol/1 diavalent cations. Long-term storage of mixtures containing Freamine II is not recommended because of an interaction between the emulsifier and the amino acids. In a small open trial patients maintained their serum albumin concentrations. There was no evidence of impaired pulmonary function even in those subjects with impaired fat clearance.

Journal Article↗
PubMed1989

Role of amino acids in stimulation of postprandial insulin, glucagon, and pancreatic polypeptide in humans.

Protein-rich meals stimulate secretion of insulin, glucagon, and pancreatic polypeptide (PP) from the endocrine pancreas. On the one hand, this is due to increased levels of circulating amino acids, and, on the other, neural and/or endocrine factors can contribute to activation of islet cell function. The present study was designed to determine, first, pancreatic endocrine function and postprandial amino acid levels after a protein and a protein-carbohydrate meal and second, insulin, glucagon, and PP levels during infusion of amino acid mixtures that imitate the postprandial amino acid pattern. In healthy volunteers the ingestion of a protein-rich meal (300 g tenderloin steak) elicited within 1 h an increase of virtually all amino acids by 20-400 mumol/L above basal values. The infusion of two different amino acid solutions available for use in humans showed that Aminosteril-N-Hepa (AS) was better for the imitation of the so-called "insulinogenic" amino acids while Aminoplasmal L-10 (AP) gave more comparable plasma levels of the "glucagonogenic" amino acids. Both solutions were not able to imitate the postprandial amino acid pattern completely. With regard to insulin levels, both solutions gave a comparable increase, while AP but not AS stimulated glucagon and PP levels. This suggests that circulating amino acids may be responsible for 60% of the postprandial insulin response after a protein meal, while their contribution to glucagon release can only be roughly estimated at 30-60%. The contribution of circulating nutrients to the greater insulin response after the protein-carbohydrate meal was comparable (60%), while the attenuated glucagon response can be ascribed almost completely to the effect of circulating nutrients. In conclusion, the present data demonstrate that the composition of amino acid mixtures is as yet not ideal for a complete imitation of the postprandial amino acid pattern. The insulin, glucagon, and PP response depends on the amino acid mixtures and accordingly the respective plasma amino acid concentrations obtained during infusion studies. The adequate imitation of plasma amino acid levels is of critical importance for the evaluation of absorbed and circulating amino acid effects in the postprandial state.

Adult↗