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Biomedical subjects

D Burston

Publications and source records attributed to D Burston.

At least 37 records · Page 2Linked to original sources
PubMed1979

Intestinal handling of two tetrapeptides by rodent small intestine in vitro.

Uptake of free Leu and Ala and uptake of these amino acids from the tetrapeptides Leu-Gly-Gly-Gly and Ala-Gly-Gly-Gly has been studied in rings of everted rodent jejunum in vitro. When mediated uptake of free Leu was virtually saturated addition of Leu-Gly-Gly-Gly gave no significant increase in uptake of Leu. Uptake of Leu and of Ala from the tetrapeptides was strongly inhibited by Met, as was uptake of these amino acids from free solution. The results did not suggest that either tetrapeptide was taken up intact by the jejunum.

Alanine↗
PubMed1979

Kinetics of mucosal influx of glycylsarcosine, glycine and leucine into hamster jejunum and ileum in vitro.

1. This paper describes an investigation of the kinetics of influx of the dipeptide glycylsarcosine and the amino acids glycine and L-leucine into rings of everted hamster small intestine in vitro, in proximal and distal small intestine (jejunum and ileum). Results were expressed per unit wet weight of intestine. 2. At all concentrations studied (0.1--100 mmol/l), influx of glycylsarcosine was more rapid in the jejunum than in the ileum. In contrast, at all concentrations studied, influx of glycine and leucine was more rapid in the ileum than the jejunum. 3. Estimates of the simple diffusion component in total influx were made. This component became increasingly large as the substrate concentration was raised. After correction for simple diffusion, transport of all three substrates conformed to Michaelis-Menten kinetics in both jejunum and ileum. Values for simple diffusion, apparent Kt and Vmax, are reported. 4. Possibly physiological implications of the results are discussed, and it is pointed out that under experimental conditions similar to our own, simple diffusion is too large a component in total influx to be ignored.

Animals↗
PubMed1978

The absorption by human volunteers of glutamic acid from monosodium glutamate and from a partial enzymic hydrolysate of casein.

Peripheral plasma concentrations of glutamic and aspartic acids and alanine were measured after ingestion of monosodium glutamate or a pancreatic hydrolysate of casein by human volunteers. The doses of each material were such that they contained similar amounts of glutamic acid. Plasma glutamic acid concentrations rose promptly after the monosodium glutamate but mean peak concentrations were well below those likely to cause neurological damage. Plasma aspartic acid concentrations also rose after the monosodium glutamate but the behaviour of plasma alanine concentrations suggested that intestinal transamination of glutamic acid was insufficient to cause an appreciable rise in alanine concentration in the peripheral plasma. Significant increments in plasma glutamic acid concentrations did not occur after the pancreatic hydrolysate of casein and it is probable that competition for absorptive mechanisms by other amino acids, both free and peptide-bound, causes absorption of glutamic acid to be slower from mixtures of peptides and amino acids than from monosodium glutamate itself.

Absorption↗
PubMed1978

Uptake of glycylglycine by the scutellum of germinating barley grain.

The scutella separated from germinating barley grains (Hordeum vulgare L. cv. Himalaya) took up the dipeptide [(14)C]glycylglycine (Gly-Gly) rapidly from incubation media. The pH optimum of the process was about 4.5, and the rate of uptake conformed to Michaelis-Menten kinetics with an apparent K(m) of 2.3 mm and V(max) of 41 mumole gram(-1) hour(-1). The uptake was strongly inhibited by dinitrophenol and cyanide and by lack of O(2).After incubation of the scutella with Gly-Gly, no intact Gly-Gly was detectable in the scutella but the level of free glycine increased. The poorly hydrolyzed "model" dipeptide glycylsarcosine, which is actively taken up and accumulated by the scutella, was a competitive inhibitor of the uptake of Gly-Gly and completely inhibited the uptake at infinitely high inhibitor concentration. This suggests that Gly-Gly is taken up by the same mechanism as glycylsarcosine as an intact dipeptide (without hydrolysis in the membrane) and is hydrolyzed to free glycine by the abundant peptidases of the scutella.The uptake of Gly-Gly was not affected by glycine or leucine, but was strongly inhibited by all of the 10 dipeptides tested for inhibition. The three dipeptides tested for uptake, Ala-Gly, Pro-Gly, and Gly-Pro, were all taken up by the scutella. Thus, the uptake mechanism for the dipeptides seems to be rather nonspecific with respect to the side chains of the amino acids. The high rates of the uptake suggest that this process has an essential role in the mobilization of reserve proteins in the germinating grain.

Journal Article↗
PubMed1977

Amino acid concentrations in portal venous plasma during absorption from the small intestine of the guinea pig of an amino acid mixture simulating casein and a partial enzymic hydrolysate of casein.

1. The characteristics of absorption of individual amino acids from amino acid mixtures simulating casein and from enzymic hydrolysates of casein containing oligopeptides as well as free amino acids are known to be different. The differences, which are attributable to mucosal uptake of small peptides, involve more rapid absorption from the enzymic hydrolysates of certain amino acids which are relatively slowly absorbed from the amino acid mixtures. This could lead to more effective utilization of amino acids from the enzymic hydrolysates than from the amino acid mixtures. 2. To obtain further information bearing on this hypothesis, we have used a recently developed technique for portal cannulation in the guinea pig to make a preliminary investigation of amino acid concentrations in the portal venous plasma at intervals after the infusion into the duodenum of equivalent amounts of (a) an amino acid mixture simulating casein and (b) a partial enzymic (papain followed by kidney peptidases) hydrolysate of casein, the two preparations being infused in separate experiments. 3. For some amino acids, such as leucine, isoleucine, valine, phenylalanine and lysine, the curves after the enzymic hydrolysate were fairly similar to the corresponding curves after the amino acid mixture, though usually slightly lower. With other amino acids, the curves after the enzymic hydrolysate were very much lower than the corresponding curves after the amino acid mixture. With serine, glutamine, proline and glycine this discrepancy was particularly great. 4. The results cannot yet be fully explained, but their main features are explicable by the hypothesis that the lower amino acid concentrations in portal plasma after the enzymic hydrolysate are the result of entry of amino acids into the portal blood in peptide form, in which they would not be detectable by the analytical technique employed, and possibly also of more rapid clearance of amino acids from the blood during absorption of this preparation.

Amino Acids↗
PubMed1977

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.

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, glutamin 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.

Adult↗
PubMed1976

Intestinal absorption of amino acids and peptides in Hartnup disorder.

Absorption of free and peptide-bound amino acids was investigated in a girl with Hartnup disorder aged 26 months. Plasma levels of amino acids were followed after oral administration of (1) an amino acid mixture simulating casein and (2) an equivalent dose of a partial enzymic hydrolysate of casein containing oligopeptides in addition to free amino acids. The results suggested that many neutral amino acids were poorly absorbed when given in the free form, but much more readily absorbed when given as peptides. Unexpectedly, the results also suggested that glutamic acid was poorly absorbed when given in the free form. The results obtained with threonine could not be interpreted. There was an increased renal clearance of many neutral amino acids, including glycine, but clearance of proline was not increased. Most amino acids with an increased renal clearance also appeared to be poorly absorbed when given by mouth in the free form.

Amino Acids↗
PubMed1976

Evidence for a single common carrier for uptake of a dipeptide and a tripeptide by hamster jejunum in vitro.

This paper describes an investigation of whether a dipeptide and a tripeptide were taken up by hamster jejunum by the same transport system, or whether there was evidence of uptake by more than one transport system. The work was carried out with rings of everted hamster jejunum in vitro, under conditions of influx, using the "model" peptides glycylsarcosine, glycylsarcosylsarcosine, and glycylsarcosylsarcosylsarcosine. These peptides are all exceptionally resistant to hydrolysis, appearing intact in the rings, and the di- and tripeptide have previously been shown to be concentrated in the rings by active transport. The results showed that influx of glycylsarcosine was inhibited by glycylsarcosylsarcosine in a competitive way, and that each of the peptides was capable of causing virtually complete inhibition of influx of the other. Glycylsarcosylsarcosylsarcosine had no effect on influx of glycylsarcosine or of glycylsarcosylsarcosine. It was concluded that although the existence of multiple transport systems shared by both glycylsarcosine and glycylsarcosylsarcosine could not be ruled out, the simplest hypothesis was that both the dipeptide and the tripeptide shared a single common carrier for uptake. The tetrapeptide glycylsarcosylsarcosylsarcosine was apparently not transported by this carrier, in agreement with previous results. The possible effects of the "unstirred layer" were taken into account in considering the results and are discussed. They do not alter the conclusions reached.

Animals↗
PubMed1975

Changes in plasma amino acid concentrations in man after ingestion of an amino acid mixture simulating casein, and a tryptic hydrolysate of casein.

1. Plasma amino acid levels have been estimated at 0, 15, 30 and 45 min after ingestion of doses of (1) an amino acid mixture simulating casein and (2) a tryptic hydrolysate of casein consisting mainly of oligopeptides. Both doses contained the same amount of nitrogen. 2. After ingestion of both preparations, there was a prompt increase in plasma amino acid levels, followed by a decrease. No such change occurred in fasting subjects. There were no significant differences between increments in plasma amino acid levels after ingestion of the amino acid mixture and the corresponding increments after ingestion of the tryptic hydrolysate. 3. Correlations were found between the areas under the curves for individual amino acid concentrations, after ingestion of the two preparations, and the amino acid composition of casein. The results do not suggest that increases in plasma amino acid levels following small doses of protein digestion products are the result of circadian changes, or that such increases are 'swamped' by absorption of amino acids from endogenous protein in the lumen of the small intestine.

Adult↗
PubMed1975

Evidence for active transport of tripeptides by hamster jejunum in vitro.

1. This paper describes the uptake by rings of everted hamster jejunum in vitro of three peptides with structural features making them resistant to hydrolysis, glycylsarcosylsarcosine, glycylsarcosylsarcosylsarcosine and beta-alanylglycylglycine. 2. Glycylsarcosylsarcosine was taken up by a saturable mechanism and accumulated intact in the intracellular compartment of the intestinal wall, apparently against an electrochemical gradient. Its uptake was reduced by Na+-replacement, anoxia and metabolic inhibitors. It was concluded that uptake of this peptide was the result of Na+-dependent active transport. 3. Glycylsarcosylsarcosylsarcosine was very poorly taken up and its uptake did not appear to be the result of active transport. 4. Beta-Alanylglycylglycine appeared intact in the intracellular compartment of the intestinal wall on a substantial scale though it was not concentrated. No satisfactory evidence of uptake by a saturable mechanism was obtained. Uptake was, however, inhibited by anoxia, 2,4-dinitrophenol and Na+-replacement. Reasons are given for supposing that uptake of this peptide may be the result of Na+-dependent active transport by the same carrier as that utilized by glycylsarcosylsarcosine. 5. The results suggest that provided that they escape brush-border hydrolysis, tripeptides, like dipeptides, are actively transported into the absorptive cells of the intestinal mucosa, but that the ability of these cells to take up peptides by an active mechanism is unlikely to extend to tetrapeptides.

Alanine↗
PubMed1975

A common mechanism for transport of di- and tri-peptides by hamster jejunum in vitro.

1. This paper describes the results of a survey of the effects of peptides and amino acids on uptake by rings of everted hamster jejunum in vitro of glycylsarcosylsarcosine, a tripeptide which is taken up by an active mechanism but is very resistant to hydrolysis, appearing intact in the rings. The results of a small number of similar experiments with beta-alanylglycylglycine, another tripeptide which is taken up with very little hydrolysis, are also described. 2. Uptake of the two tripeptides was inhibited by other di- and tri-peptides, but not by free amino acids. The results suggest that dipeptides and tripeptides share a common uptake mechanism. The tetrapeptide glycylsarcosylsarcosylsarcosine did not inhibit uptake of glycylsarcosylsarcosine, and appears to be unable to utilize the uptake mechanism. 3. The results add to information about the influence of molecular structure on intestinal uptake of peptides by the system used by glycylsarcosylsarcosine, which is shared by a wide range of other di- and tri-peptides. In conjunction with previous results, they suggest that substitution of the N-terminal amino or C-terminal carboxyl groups reduces affinity for transport, that the presence of a beta-amino acid residue in a peptide is tolerated by the transport system, and that the presence of a D-amino acid residue reduces affinity for transport. Some peptides containing or made up of basic or acidic amino acid residues appear to have a low affinity for the transport system used by glycylsarcosylsarcosine. 4. Of two biologically active peptides, one, cephalexin, a peptide antibiotic, inhibited uptake of glycylsarcosylsarcosine and is probably transported by the same system. The other, prolylleucylglycineamide, which has the action of a hypothalamic regulatory factor, did not, and its structural features may make it unsuitable for carrier-mediated transport by the small intestine.

Animals↗
PubMed1975

Jejunal absorption of an amino acid mixture simulating casein and an enzymic hydrolysate of casein prepared for oral administration to normal adults.

1. An intestinal perfusion technique was used in six normal human subjects to study absorption of sixteen individual amino acids from an amino acid mixture simulating casein and from an enzymic hydrolysate of casein, prepared for oral administration to these subjects, which consisted of a mixture of oligopeptides and free amino acids. 2. Total absorption of alpha-amino nitrogen was greater from the casein hydrolysate than from the amino acid mixture, and the considerable variation in percentage absorption of individual amino acids from the amino acid mixture was much reduced when the enzymic hydrolysate solution was perfused, as a number of amino acids which were poorly absorbed from the amino acid mixture were absorbed to a greater extent from the casein hydrolysate. 3. These findings indicate that after extensive intestinal resections or in malabsorption there might be significant nutritional advantages in the administration of protein hydrolysates rather than amino acid mixtures.

Administration, Oral↗