scholarly journals Comparison of the isotope dilution method for determination of the ileal endogenous amino acid losses with labelled diet and labelled pigs

2000 ◽  
Vol 83 (2) ◽  
pp. 123-130 ◽  
Author(s):  
Vincent Hess ◽  
Philippe Ganier ◽  
Jean-Noel Thibault ◽  
Bernard Sève
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Latin Square ◽  
Isotope Dilution Method ◽  
Dilution Method ◽  
First Case ◽  
Endogenous Protein ◽  
The Individual ◽  
Protein Free Diet

The aims of the present study were first to compare the amino acid dilution method performed using labelled animals with that using labelled diets, and second to determine real digestibilities and total ileal endogenous losses of N and amino acids. Two diets containing pea cultivars (Solara and Amino) and a protein-free diet were compared in a 3 × 3 Latin-square experiment. The three pigs were each prepared with an ileo-rectal anastomosis and were continuously infused with [1-13C]leucine. For each cultivar,15N-labelled and unlabelled diets were formulated. The real digestibility and endogenous losses of leucine were higher when obtained by labelling the pig than by labelling the foodstuff. This was due either to the inadequate estimation of the endogenous protein enrichment in the first case or to the importance of dietary N recycling in the second case. However, in both cases the ileal endogenous losses of N and amino acids were higher than the basal losses determined with the protein-free diet. There were significant differences between the two pea cultivars in terms of phenylalanine and leucine when measured with labelled diets. It is suggested that, although ileal endogenous losses may be underestimated, using labelled feedstuffs is of great interest due to the direct estimation of the individual amounts of amino acids.

scholarly journals Digestion of protein in small and large intestine of the pig

1974 ◽  
Vol 32 (3) ◽  
pp. 479-489 ◽  
Author(s):  
J. H. G. Holmes ◽  
H. S. Bayley ◽  
P. A. Leadbeater ◽  
F. D. Horney
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Amino Acid ◽  
Large Intestine ◽  
Dry Matter ◽  
Latin Square ◽  
Rapeseed Meal ◽  
Total Amino Acid ◽  
Acid Fermentation ◽  
Protein Free Diet

1. Six 45 kg pigs with re-entrant ileal cannulas were used in two 3 × 3 Latin-square design experiments to study the site of absorption of protein and amino acids. Semi-purified diets containing soya-bean meal (SBM), rapeseed meal (RSM) or no protein source (protein-free) were offered at the rate of 1 kg dry matter/d.2. Flow-rates of ileal contents for 24 h collection periods, corrected for recovery of marker, were 3135, 3127 and 1243 ml (SE 390) for SBM, RSM and protein-free diets respectively.3. Amounts of dry matter digested in the small intestine were 730, 669 and 809 g/d for SBM, RSM and protein-free diets respectively, all values being significantly different (P < 0·001).4. Nitrogen intakes were 32·6, 29·9 and 5·9 g/d, and amounts digested in the small intestine were 25·7, 20·2 and 1·6 g/d for SBM, RSM and protein-free diets respectively, all values being significantly different (P < 0·001). Amounts digested in the large intestine were 2·6, 3·7 and 0·7 g/d.5. Total amino acid intakes and amounts collected at the ileum and in the faeces were (g/d): SBM, 177, 24 and 18; RSM, 149, 28 and 22; protein-free 3, 9 and 12. Digestibility in the small intestine was higher for SBM than RSM for seventeen of the eighteen amino acids estimated. Greater quantities of arginine, methionine, cystine and tyrosine were voided in the faeces than passed through the ileal cannulas for pigs receiving the SBM and RSM diets. For those receiving the protein-free diet this was true for each amino acid except proline.6. Significant differences were found between all diets in the concentration of some amino acids in ileal and faecal amino-N, and endogenous protein secretions did not mask the differences between diets.7. Differences in digestibility between SBM and RSM were greater at the ileum than in the faeces. Amino acid fermentation in the large intestine obscured or reduced differences between SBM and RSM.

scholarly journals DEVELOPMENT OF ANALYTICAL METHOD FOR THE DETERMINATION OF NINHYDRIN-POSITIVE SUBSTANCES IN AMINO ACIDS BY HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY

2018 ◽  
Vol 11 ◽  
Author(s):  
Srinivasa Rajagopalachari Nk ◽  
Shanmugasundaram P
Keyword(s):  
Amino Acids ◽  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Amino Acid ◽  
High Performance ◽  
Hplc Method ◽  
Drug Products ◽  
Cation Exchange Column ◽  
The Individual

Aim and Objectives: The aim of the work is focused on the optimization of the high-performance liquid chromatography (HPLC) method for the determination of ninhydrin-positive substances in amino acids using HPLC technique in a single method. Since, most of the amino acids are widely used in the determination of Renal and Nutrition drug products exist independently in the monograph for each amino acid either by TLC or HPLC.Methods: The chromatographic separation was performed using sodium amino acid analysis cation exchange column using Sodium Eluent Na 315, Sodium eluent Na 425, and Sodium Eluent Na 640 as Mobile phase, performed by gradient program with detection of wavelength 570 nm using flow rate as 0.4 mL/min. The method has been evaluated using post-column derivatization technique (HPLC/Pinnacle PCX).Results: All the amino acids were eluted correspondingly at the individual retention time and the method shall be validated as per the ICH Q2R1 Guideline.Conclusion: The method has been successfully evaluated and developed for the analytical applications.

A RAPID COLORIMETRIC METHOD FOR THE DETERMINATION OF LYSINE IN PROTEIN HYDROLYSATES

1947 ◽  
Vol 25b (6) ◽  
pp. 540-547 ◽  
Author(s):  
M. Boulet ◽  
J. A. Nelson ◽  
W. D. McFarlane
Keyword(s):  
Amino Acids ◽  
Colorimetric Method ◽  
Color Reaction ◽  
Isotope Dilution Method ◽  
Dilution Method ◽  
Blue Color ◽  
Lysine Content ◽  
Microbiological Methods ◽  
Gelatin Hydrolysate

A solution of chlorinated lysine develops a blue color when heated with phosphomolybdic–phosphotungstic acid. This color reaction, which will detect lysine at a concentration of 1 p.p.m., has been made the basis of a sensitive and rapid colorimetric method for the determination of lysine. Lysine and arginine are quantitatively separated from the other amino acids in a protein hydrolysate by adsorption on Decalso and the lysine content of the eluate is determined in the presence of arginine (which does not give the color reaction) by applying the color reaction after chlorination. Satisfactory recoveries of added lysine have been obtained from mixtures of amino acids and from a gelatin hydrolysate. The lysine content of several proteins has been determined and the results compared with those in the literature. In general the values obtained by the colorimetric method are intermediate between those obtained by isolation procedures and those by microbiological methods. The result of a determination on crystalline bovine serum albumin checked closely with the value obtained by the isotope dilution method.

scholarly journals Endogenous flow of amino acids in the avian ileum as influenced by increasing dietary peptide concentrations

2008 ◽  
Vol 101 (6) ◽  
pp. 822-828 ◽  
Author(s):  
Velmurugu Ravindran ◽  
Patrick C. H. Morel ◽  
Shane M. Rutherfurd ◽  
Donald V. Thomas
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Broiler Chickens ◽  
Amino Acid Profile ◽  
Dependent Manner ◽  
Endogenous Protein ◽  
High Concentrations ◽  
Protein Free Diet ◽  
Endogenous Amino Acid

The aim of the present study was to establish whether feeding broiler chickens with diets containing increasing dietary peptide concentrations would cause increases in ileal endogenous amino acid flow. The flow of N and most amino acids increased quadratically (P < 0·05 to 0·001) with increasing dietary concentrations of peptides. The exceptions were the flow of threonine, serine, glycine, tyrosine and cystine, which increased linearly (P < 0·001) with dietary peptide levels. Another notable exception to the general trend was the flow of proline, which was significantly higher (P < 0·01) in birds fed the protein-free diet. The amino acid profile of endogenous protein, expressed as proportion of crude protein, indicated that the ratios of threonine, glutamic acid, proline, glycine, leucine, histidine, arginine and cystine were influenced (P < 0·05) with increasing dietary peptide concentrations. In general, compared with the protein-free diet, the ratios of threonine and arginine in endogenous protein were lower (P < 0·05) and those of glutamic acid, glycine and histidine were greater (P < 0·05) in diets with high concentrations of peptides. The ratio of proline was found to decrease (P < 0·05) with increasing dietary peptide concentrations. These changes in the amino acid profile of endogenous protein are probably reflective of changes in the output of one or more of the components of endogenous protein. Overall, the present results demonstrated that increasing dietary peptide concentrations increased the flow of endogenous amino acid flow at the terminal ileum of broiler chickens in a dose-dependent manner and also caused changes in the composition of endogenous protein. The observed changes in endogenous amino flow will influence the maintenance requirements for amino acids and also have implications for the calculation of true digestibility coefficient of feedstuffs.

Recovery and composition of endogenous protein collected at the terminal ileum as influenced by the age of broiler chickens

2004 ◽  
Vol 55 (6) ◽  
pp. 705 ◽  
Author(s):  
V. Ravindran ◽  
W. H. Hendriks
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Terminal Ileum ◽  
Broiler Chickens ◽  
Age Groups ◽  
Amino Acid Profile ◽  
Endogenous Protein ◽  
True Digestibility ◽  
The Individual ◽  
Two Age Groups

The recovery and composition of endogenous protein at the terminal ileum of broiler chickens were determined at 14 and 42 days post-hatching using the peptide alimentation method. The ileal endogenous flows of nitrogen and amino acids, expressed as mg/kg dry matter intake, differed (P < 0.05–0.01) between the two age groups, with flows increasing with age, except for lysine, histidine and glycine. The flows of lysine and histidine were unaffected (P > 0.05) by age, whereas a tendency (P = 0.07) for increased loss with age was observed for glycine. The amino acid profile of ileal endogenous protein, expressed as g/100 g crude protein, did not differ (P > 0.05) between 14-day- and 42-day-old broilers, suggesting that the relative proportions of the individual sources that contribute to the endogenous protein were similar at both ages. In both age groups, the most abundant amino acids in the ileal endogenous protein were glutamic acid, aspartic acid, proline, serine, glycine, and threonine. The present findings suggest that, when determining true digestibility, corrections using endogenous amino acid flows determined with broilers of a particular age to apparent amino acid digestibility values determined with birds of a different age would clearly result in less accurate true digestibility estimates.

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