Characterization of whole body compositional growth of male ducks during the twenty-nine day post-hatch period

2013 ◽  
Vol 93 (1) ◽  
pp. 113-122 ◽  
Author(s):  
A. P. Schinckel ◽  
M. E. Einstein ◽  
K. M. Ajuwon ◽  
O. Adeola
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dry Matter ◽  
The Body ◽  
Whole Body ◽  
Nutrient Requirements ◽  
Accretion Rates ◽  
Indispensable Amino Acids ◽  
Hatch Period

Schinckel, A. P., Einstein, M. E., Ajuwon, K. M. and Adeola, O. 2013. Characterization of whole body compositional growth of male ducks during the twenty-nine day post-hatch period. Can. J. Anim. Sci. 93: 113–122. Changes in whole body dry matter, lipid, ash, energy, crude protein, and amino acids were evaluated during a 29 d post-hatch period in White Pekin ducks. Drakes were assigned to slaughter 1, 8, 15, 22, or 29 d post-hatch with four replicates of four ducks per slaughter period. The body weight (BW) data were fitted to the Weibull function with the form:[Formula: see text]where BWit is the BW of the ith duck at t days of age and A, B, C, and IP are parameters. The value of IP, the inflection point, which minimized the residual SD, was 40 d. Values of A (8591 g, SE=190), B (42.87, SE=11.5), and C (1.7399, SE=0.050) resulted in an R 2 of 0.9836 and residual SD of 83.7 g. Allometric (Y=A BWB), linear-quadratic and exponential (Y=exp (b0+b1BW+b2 (BW)2) functions of BW were fitted to the chemical component and amino acid mass data. Dry matter percentage of the ducks increased (P<0.01) with age. The protein content of the dry matter decreased (P<0.01) from day 1 to day 8 (69 to 58.2%) and then increased to 60% by d 29. Concentrations of several amino acids were affected (P<0.05) by age. The predicted accretion rates of Lys, Trp, and Met relative to protein accretion increased as age increased. The predicted daily accretion rates for major indispensable amino acids increased rapidly the first 5 d post-hatch and subsequently increased but at a decreasing rate to day 29 post-hatch. The relative growth rates of chemical components and indispensable amino acids were affected by age indicating that the nutrient requirements of ducks differ from day 1 to day 29 post-hatch. Compositional growth and amino acid accretion data can be used to model the nutrient requirements of ducks.

scholarly journals In vivo Determination of Amino Acid Bioavailability in Humans and Model Animals

2005 ◽  
Vol 88 (3) ◽  
pp. 923-934 ◽  
Author(s):  
Malcolm F Fuller ◽  
Daniel Tomé
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
The Body ◽  
Whole Body ◽  
Intestinal Lumen ◽  
Stable Isotope Labelling ◽  
Ileal Digestibility ◽  
Hydrolyzed Protein ◽  
Protein Free Diet

Abstract Because the digestion of many dietary proteins is incomplete, and because there is a continuous (but variable) entry into the intestinal lumen of endogenous protein and amino acid nitrogen that is also subject to digestion, the fluxes of nitrogen, amino acids, and protein in the gut exhibit a rather complicated pattern. Methods to distinguish and quantitate the endogenous and dietary components of nitrogen and amino acids in ileal chyme or feces include the use of a protein-free diet, the enzyme-hydrolyzed protein method, different levels of protein intake, multiple regression methods, and stable-isotope labelling of endogenous or exogenous amino acids. Assessment of bioavailability can be made, with varying degrees of difficulty, in man directly but, for routine evaluation of foods, the use of model animals is attractive for several reasons, the main ones being cost and time. Various animals and birds have been proposed as models for man but, in determining their suitability as a model, their physiological, enzymological, and microbiological differences must be considered. Fecal or ileal digestibility measurements, as well as apparent and true nitrogen and amino acid digestibility measurements, have very different nutritional significance and can, thus, be used for different objectives. Measurements at the ileal level are critical for determining amino acid losses of both dietary and endogenous origin, whereas measurements at the fecal level are critical in assessing whole-body nitrogen losses. A complementary and still unresolved aspect is to take into account the recycling of intestinal nitrogen and bacterial amino acids to the body.

Effects of i.v. amino acids on human splanchnic and whole body oxygen consumption, blood flow, and blood temperatures

1994 ◽  
Vol 266 (3) ◽  
pp. E396-E402 ◽  
Author(s):  
T. Brundin ◽  
J. Wahren
Keyword(s):  
Amino Acids ◽  
Blood Flow ◽  
Cardiac Output ◽  
Oxygen Consumption ◽  
Amino Acid ◽  
The Body ◽  
Whole Body ◽  
Acid Infusion ◽  
Amino Acid Infusion ◽  
Splanchnic Oxygen

The thermic effect of amino acid administration was examined in healthy subjects. Pulmonary and splanchnic oxygen uptake, cardiac output, splanchnic blood flow, and blood temperatures were measured in eight healthy men before and during 2.5 h of intravenous infusion of 600 kJ of a mixture of 19 amino acids. Indirect calorimetry and catheter techniques were used, including thermometry in arterial and a hepatic venous blood. During the infusion, pulmonary oxygen uptake rose progressively from a basal value of 269 +/- 6 to 321 +/- 8 ml/min after 2.5 h. The splanchnic oxygen consumption increased from a basal level of 64 +/- 4 to a peak value of 91 +/- 7 ml/min after 2 h of infusion. The 2.5 h average splanchnic proportion of the amino acid-induced whole body thermogenesis was 51 +/- 11%. Cardiac output increased from 6.2 +/- 0.3 in the basal state to 7.3 +/- 0.4 l/min, whereas the splanchnic blood flow remained unchanged during the infusion period. The arteriohepatic venous oxygen difference increased from 51 +/- 4 in the basal state to 65 +/- 5 ml/l after 2 h of amino acid infusion. The blood temperature rose by approximately 0.25 degrees C during the amino acid infusion, reflecting an increased heat accumulation in the body. It is concluded that the splanchnic tissues account for approximately one-half of the amino acid-induced whole body thermogenesis, that amino acid infusion augments blood flow in the extrasplanchnic but not in the splanchnic tissues, and stimulates the accumulation of heat in the body most likely via a resetting of the central thermosensors.

scholarly journals Maintenance threonine requirement and efficiency of its use for accretion of whole-body threonine and protein in young chicks

1997 ◽  
Vol 78 (1) ◽  
pp. 111-119 ◽  
Author(s):  
Hardy M Edwards III ◽  
David H Baker ◽  
Sergio R Fernandez ◽  
Carl M Parsons
Keyword(s):  
Amino Acids ◽  
Weight Gain ◽  
Amino Acid ◽  
Feed Efficiency ◽  
Regression Line ◽  
Whole Body ◽  
Broiler Chicks ◽  
Body Protein ◽  
Maximal Weight ◽  
Indispensable Amino Acids

Broiler chicks were fed on chemically-defined crystalline amino acid diets containing graded levels of L-threonine (Thr) during the period 10–20 d post-hatching. Doses of Thr represented 5,10,15,40,55,70 and 95% of its ideal level for maximal weight gain and feed efficiency. Other amino acids were maintained at minimized excess levels that were 15% (of ideal) above the various doses of Thr. Following 10d of feeding and a 24h fast, chicks were killed for whole-body protein and amino acid analysis. Using pen accretion means, weight gain (r20·98), protein accretion (r2 0·99), and Thr accretion (r2 0·99) were linear (P<0·01) functions of Thr intake. Slope of the Thr accretion regression line indicated that 82% of the Thr intake was recovered in whole-body protein. At zero Thr intake, chicks lost 11·9 mg Thr/d. The Thr maintenance requirement was 45·7 mg/d per kg body weight 0·75. Increasing doses of Thr resulted in increased (P<0·05) concentrations of methionine, isoleucine, histidine and lysine in whole-body protein. Other indispensable amino acids, including Thr, also tended to increase. Whole-body glycine, proline, serine and cystine concentrations decreased (P<0·05) as Thr was increased in the diet. The maintenance need for Thr represented 5·5% of the total need for Thr. The data suggest that efficiency of Thr utilization is constant at all levels of Thr intake between 5 and 95% of the level required for maximal weight gain and feed efficiency.

scholarly journals Available versus digestible amino acids – new stable isotope methods

2012 ◽  
Vol 108 (S2) ◽  
pp. S306-S314 ◽  
Author(s):  
Rajavel Elango ◽  
Crystal Levesque ◽  
Ronald O. Ball ◽  
Paul B. Pencharz
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Stable Isotope ◽  
Growing Pigs ◽  
The Body ◽  
Whole Body ◽  
Food Protein ◽  
Adult Humans

The nutritive value of food protein sources is dependent on the amino acid composition and the bioavailability of the nutritionally indispensable amino acids. Traditionally the methods developed to determine amino acid bioavailability have focused on intestinal absorption or digestibility, which is calculated as the percent of amino acid intake that does not appear in digesta or faeces. Traditional digestibility based methods do not always account for gut endogenous amino acid losses or absorbed amino acids which are unavailable due to the effect of heat processing and the presence of anti-nutritional factors, though methods have been developed to address these issues. Furthermore, digestibility based methods require the use of animal models, thus there is a need to developin vivomethods that can be applied directly in human subjects to identify the proportion of dietary amino acids which is bioavailable, or metabolically available to the body for protein synthesis following digestion and absorption. The indicator amino acid oxidation (IAAO) method developed in our laboratory for humans has been systematically applied to determine almost all indispensable amino acid requirements in adult humans. Oxidation of the indicator amino acid is inversely proportional to whole body protein synthesis and responds rapidly to changes in the bioavailability of amino acids for metabolic processes. Using the IAAO concept, we developed a newin vivomethod in growing pigs, pregnant sows and adult humans to identify the metabolic availability of amino acids in foods. The stable isotope based metabolic availability method is suitable for rapid and routine analysis in humans, and can be used to integrate amino acid requirement data with dietary amino acid availability of foods.

scholarly journals Avoided motifs: short amino acid strings missing from protein datasets

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Pablo Mier ◽  
Miguel A. Andrade-Navarro
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Function ◽  
Large Protein ◽  
New Approach ◽  
Cellular Context ◽  
Human Proteins ◽  
Context Specific ◽  
Protein Datasets

Abstract According to the amino acid composition of natural proteins, it could be expected that all possible sequences of three or four amino acids will occur at least once in large protein datasets purely by chance. However, in some species or cellular context, specific short amino acid motifs are missing due to unknown reasons. We describe these as Avoided Motifs, short amino acid combinations missing from biological sequences. Here we identify 209 human and 154 bacterial Avoided Motifs of length four amino acids, and discuss their possible functionality according to their presence in other species. Furthermore, we determine two Avoided Motifs of length three amino acids in human proteins specifically located in the cytoplasm, and two more in secreted proteins. Our results support the hypothesis that the characterization of Avoided Motifs in particular contexts can provide us with information about functional motifs, pointing to a new approach in the use of molecular sequences for the discovery of protein function.

Characterization of an isozyme of S-adenosylmethionine synthetase from rat liver

1984 ◽  
Vol 62 (5) ◽  
pp. 276-279 ◽  
Author(s):  
C. H. Lin ◽  
W. Chung ◽  
K. P. Strickland ◽  
A. J. Hudson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Enzymatic Synthesis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Aromatic Amino Acids ◽  
Adenosylmethionine Synthetase ◽  
Cellulose Column

An isozyme of S-adenosylmethionine synthetase has been purified to homogeneity by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and gel filtration on a Sephadex G-200 column. The purified enzyme is very unstable and has a molecular weight of 120 000 consisting of two identical subunits. Amino acid analysis on the purified enzyme showed glycine, glutamate, and aspartate to be the most abundant and the aromatic amino acids to be the least abundant. It possesses tripolyphosphatase activity which can be stimulated five to six times by S-adenosylmethionine (20–40 μM). The findings support the conclusion that an enzyme-bound tripolyphosphate is an obligatory intermediate in the enzymatic synthesis of S-adenosylmethionine from ATP and methionine.

PSVI-13 Amino Acid Supplementation During the Adaptation Period Did Not Affect the Standardized Ileal Digestibility of Amino Acids in Corn and Soybean Meal Fed to Pigs

2021 ◽  
Vol 99 (Supplement_1) ◽  
pp. 200-201
Author(s):  
Hyunjun Choi ◽  
Sun Jong You ◽  
Beob Gyun G Kim
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Soybean Meal ◽  
Latin Square ◽  
Sole Source ◽  
Adaptation Period ◽  
Amino Acid Supplementation ◽  
Ileal Digestibility ◽  
Indispensable Amino Acids ◽  
Dietary Treatments

Abstract The objective was to determine the influence of amino acid (AA) supplementation during the adaptation period on the ileal digestibility of crude protein and AA in corn and soybean meal (SBM). Six barrows with an initial body weight of 30.9 ± 2.6 kg fitted with a T-cannula in the distal ileum were assigned to a 6 × 6 Latin square design with 6 dietary treatments and 6 periods. Two experimental diets contained corn or SBM as the sole source of AA and an N-free diet was additionally prepared. For AA supplementation groups, an AA mixture consisted of Gly, Lys, Met, Thr, Trp, Ile, Val, His, and Phe was added to the corn diet and the N-free diet at the expense of cornstarch, and an AA mixture of Lys, Met, and Thr was added to the SBM diet. All diets contained 0.5% of chromic oxide. The 6 experimental diets were fed to the pigs for 4 and half days, and the 3 diets containing AA mixture were switched to the respective diets without AA mixture during the following 2 and half days. Ileal digesta were collected during the last 2 days. The addition of AA mixture during the adaptation period caused increased apparent ileal digestibility of Arg and Trp in corn (P &lt; 0.05), but did not affect that in SBM. The addition of AA mixture during the adaptation period caused increased apparent ileal digestibility of Pro and Gly regardless of feed ingredient (P &lt; 0.05), but did not affect that of other AA. All AA except Pro in corn and SBM were unaffected by the addition of AA mixture during the adaptation period. In conclusion, the addition of amino acid during the adaptation period does not affect the standardized ileal digestibility of indispensable amino acids in feed ingredients.

EFFECTS OF LYSINE INFUSION PER ABOMASUM OF STEERS FED CONTINUOUSLY

1972 ◽  
Vol 52 (4) ◽  
pp. 681-687 ◽  
Author(s):  
R. J. BOILA ◽  
T. J. DEVLIN
Keyword(s):  
Amino Acid ◽  
Crude Protein ◽  
Dry Matter ◽  
Latin Square ◽  
Linear Increase ◽  
The Body ◽  
The Other ◽  
Body Tissue ◽  
Rumen Microorganisms

Four dairy steers were allotted to four lysine infusion levels in a 4 × 4 latin square design and fed an 11.5% crude protein (90% dry matter (DM)) diet continuously (10-min intervals every 24 hr). Lysine hydrochloride equivalent to 0.0, 3.0, 6.0, and 9.0 g lysine per day was infused per abomasum. When 9 g lysine were infused per day, the percent of absorbed nitrogen (N) retained was significantly (P < 0.05) reduced; urinary N excretion as a percentage of N intake and plasma-free lysine were increased significantly compared with the other three infusion treatments. The infusion of 9 g lysine per day apparently exceeded the body tissue requirements for this amino acid and the excess N was excreted in the urine. A possibility of lysine being limiting (0.28% lysine of a 100% DM diet) was apparently offset by the synthesis of lysine by rumen microorganisms, which increased the dietary lysine two- to threefold. Increased levels of infused lysine did not result in a linear increase of lysine in the abomasum. With 3 g per day lysine infusion rumen ammonia and N retentions were high. However, a smaller amount of N reached the abomasum with steers on this treatment.

scholarly journals Characterization of the 6'-N-aminoglycoside acetyltransferase gene aac(6')-Im [corrected] associated with a sulI-type integron.

1997 ◽  
Vol 41 (2) ◽  
pp. 314-318 ◽  
Author(s):  
E Hannecart-Pokorni ◽  
F Depuydt ◽  
L de wit ◽  
E van Bossuyt ◽  
J Content ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Resistance Gene ◽  
Citrobacter Freundii ◽  
Gram Negative ◽  
Gene Environment ◽  
Insert Region ◽  
Klebsiella Spp

The amikacin resistance gene aac(6')-Im [corrected] from Citrobacter freundii Cf155 encoding an aminoglycoside 6'-N-acetyltransferase was characterized. The gene was identified as a coding sequence of 521 bp located down-stream from the 5' conserved segment of an integron. The sequence of this aac(6')-Im [corrected] gene corresponded to a protein of 173 amino acids which possessed 64.2% identity in a 165-amino-acid overlap with the aac(6')-Ia gene product (F.C. Tenover, D. Filpula, K.L. Phillips, and J. J. Plorde, J. Bacteriol. 170:471-473, 1988). By using PCR, the aac(6')-Im [corrected] gene could be detected in 8 of 86 gram-negative clinical isolates from two Belgian hospitals, including isolates of Citrobacter, Klebsiella spp., and Escherichia coli. PCR mapping of the aac(6')-Im [corrected] gene environment in these isolates indicated that the gene was located within a sulI-type integron; the insert region is 1,700 bases long and includes two genes cassettes, the second being ant (3")-Ib.

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