Postprandial oxidation of dietary free amino acids or egg white protein was studied using the [13CO2] breath test in rats, as well as in humans. Thirty-eight male rats were assigned to four dietary test groups. Two diets only differed in their protein fraction. Diet I contained 21% egg white protein. For the breath test egg white protein, intrinsically labelled with [1-13C]-leucine, was used as a substrate. Diet II contained the same amino acids as diet I, though not as egg white protein but in free form. Free [1-13C]-leucine was used to label this diet. In addition, two 1:1 mixtures of both diets were used. During the breath test either the free amino acid or the protein fraction was labelled as in diets I or II. The animals were breath-tested following short-term (day 5) and long-term adaptation (day 20) to their experimental diet. For all diets, including the mixed diets, postprandial oxidative losses on day 5 were significantly higher for the free leucine compared with the protein-derived leucine. Differences between free and protein-derived leucine oxidation had, however, largely disappeared on day 20. The human subjects were breath-tested without any adaptation period to the diets. The oxidative losses of free leucine were also higher than those of protein-derived leucine. None of the studies showed any indication for an interaction between the oxidation of protein-derived amino acids and free amino acids. It is concluded that free and protein-derived amino acids in the diet are mainly metabolized independently.
C]-labelled substrate. Such a non-steady state approach provides information that is complementary to the information obtained by steady-state methods using a primed continuous infusion of tracer amino acids during the fed state. In a model study with twenty adult male rats, two groups of animals were fed twice a day with one of two semi-synthetic iso-energetic diets. One diet contained egg white protein (EW) as the sole amino acid source. The second diet contained a mixture of free amino acids with a pattern similar to that of the EW diet. On day 5 of the dietary treatment, L-[1-13 C]leucine, either bound in EW protein or in free form, was ingested as part of the morning meal. The expired air was sampled at 30 min intervals for 5 h. The rate of recovery ranged from 0 % to 6 % of the dose/h. Up to 120 min after the onset of the meal, the recovery values for the free amino acid diet were higher than those for the EW diet. Differences in recovery reflect differences in postprandial utilisation. The differences in label recovery were mainly determined by the [ 13 C] enrichment of the expired air. As a consequence, CO 2 measurements are not mandatory when CO 2 production is comparable.
In the present study, the effect of free amino acid (FAA) diets on the intestinal absorption rate of methionine and leucine was studied 'ex vivo' with rats adapted for different periods of time to the diets, using the everted sac method. The adaptation period to the 21% FAA diet with an amino acid content based on casein was either, 0 (no adaptation, N-ADA), 5 (short-term adaptation, ST-ADA), or 26-33 days (long-term adaptation, LT-ADA). Within the ST-ADA and the LT-ADA groups, three different levels of methionine were included: 50%, 100% and 200% of the level normally present in casein. All diets were iso-nitrogenous and iso-caloric. After the adaptation period (0, 5, or 26-33 days), intestinal everted sacs were prepared. Methionine or leucine was added to the medium as transport substrate. The methionine absorption rate of the rats of the LT-ADA groups was higher than that of the N-ADA groups. Furthermore, adaptation to 200% dietary methionine levels caused a significantly slower leucine absorption compared to the 100%, and 50% group. Methionine absorption was similar in the 100% and 200% groups, but the absorption of methionine in the 50% group was enhanced in the distal part of the intestines. We concluded that in response diets with 21% FAAs as only amino acid source, amino acid absorption is decreased to avoid toxic effects of high levels of methionine in the circulation.
This study examined, whether the postprandial fate of dietary amino acids from different amino acid sources is regulated by the responses of insulin, glucagon, corticosterone and growth hormone (GH). Male Wistar rats were cannulated in the vena jugularis and assigned to dietary groups. The diets contained 21% casein or the same amino acids in free form. In the free amino acid diets, methionine level was varied between the groups. The feed was supplied in two distinct meals. In previous experiments it was established that oxidative amino acid losses of the free amino acid diets and protein diets were different. After 3 weeks on those diets, it appeared that the differences in postprandial oxidative losses had been diminished. GH was measured every 12 min, from 144 min before the start of the experimental meal over the following 144 min. Insulin and corticosterone were measured six times from the start of the meal until 270 min after the meal. No differences have been observed between the hormonal responses to both meals at day 5 and at day 26. In conclusion, it has been found that the differences in the oxidative losses between protein and free amino acid meals are not mediated by the combined action of the insulin, glucagon, corticosterone and GH. Postprandial catabolism of amino acids is most probably regulated by substrate induction.
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