Selection of dietary lysine and threonine concentration of growing pigs

1993 ◽  
Vol 1993 ◽  
pp. 195-195
Author(s):  
R. A. C. Fairley ◽  
S. P. Rose ◽  
M. F. Fuller
Keyword(s):  
Amino Acid ◽  
Growing Pigs ◽  
Digestible Protein ◽  
Selection Of

The aim of these trials was to discover if growing pigs can select an appropriate mixture of two feeds differing only in the level of one amino acid.A trial was conducted with 40 male pigs, with an initial mean weight of 13.1 kg. A basal low lysine feed was formulated with 172 g digestible protein (DP)/kg feed which was supplemented with synthetic lysine. The resulting feeds were similar in all respects except digestible lysine (DL) level, which was 25 (L), 50 (ML), 109 (MH) and 141 (H) g/kg DP.A second trial was carried out with threonine, using 48 male pigs with an initial mean weight of 11.94 kg. The same basal feed was supplemented with synthetic lysine to 70 g DL/kg DP and then supplemented with varying amounts of synthetic threonine to form four feeds with digestible threonine (DT) levels of 29 (L), 35 (ML), 55 (MH) and 68 (H) g/kg DP.

Agricultural practices of improve hardiness a winter-annual rape

2016 ◽  
Vol 2 (91) ◽  
pp. 57-62
Author(s):  
O.L. Kyrylesko
Keyword(s):  
Dry Matter ◽  
Agricultural Practices ◽  
Mineral Fertilizers ◽  
Farming Practices ◽  
Winter Rape ◽  
Output Capacity ◽  
Careful Preparation ◽  
Digestible Protein ◽  
Winter Annual ◽  
Selection Of

Influence of top-dressing is considered in the article, norms and terms of sowing on of winter-annual rape. The assessment conducted by the yield of green mass and seeds, output capacity by about 1 hectare of dry matter, feed units and digestible protein, the number of dead plants and density of herbage. Established that hardiness and productivity of winter rape can be enhanced through the use of farming practices as: by creating a moderate density of herbage, using optimal terms of planting and doses of mineral fertilizers, selection of predecessors and careful preparation of the soil ect. The mechanism of influence of agrotechnical receptions is exposed on of winter-annual rape through determination in roots before the offensive of the winter of separate biochemical indexes (sugar, starch, to protein).

Bioluminescent proteins prediction with voting strategy.

2020 ◽  
Vol 15 ◽  
Author(s):  
Shulin Zhao ◽  
Ying Ju ◽  
Xiucai Ye ◽  
Jun Zhang ◽  
Shuguang Han
Keyword(s):  
Amino Acid ◽  
Model Building ◽  
Prediction Method ◽  
Pair Composition ◽  
Proposed Model ◽  
Counting Rules ◽  
Significant Phenomenon ◽  
Voting Strategy ◽  
Improved Accuracy ◽  
Selection Of

Background: Bioluminescence is a unique and significant phenomenon in nature. Bioluminescence is important for the lifecycle of some organisms and is valuable in biomedical research, including for gene expression analysis and bioluminescence imaging technology.In recent years, researchers have identified a number of methods for predicting bioluminescent proteins (BLPs), which have increased in accuracy, but could be further improved. Method: In this paper, we propose a new bioluminescent proteins prediction method based on a voting algorithm. We used four methods of feature extraction based on the amino acid sequence. We extracted 314 dimensional features in total from amino acid composition, physicochemical properties and k-spacer amino acid pair composition. In order to obtain the highest MCC value to establish the optimal prediction model, then used a voting algorithm to build the model.To create the best performing model, we discuss the selection of base classifiers and vote counting rules. Results: Our proposed model achieved 93.4% accuracy, 93.4% sensitivity and 91.7% specificity in the test set, which was better than any other method. We also improved a previous prediction of bioluminescent proteins in three lineages using our model building method, resulting in greatly improved accuracy.

scholarly journals Determination and Prediction of the Amino Acid Digestibility of Sunflower Seed Meals in Growing Pigs

2014 ◽  
Vol 28 (1) ◽  
pp. 86-94 ◽  
Author(s):  
J. D. Liu ◽  
Q. Y. Li ◽  
Z. K. Zeng ◽  
P. Li ◽  
X. Xu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sunflower Seed ◽  
Growing Pigs

scholarly journals Characterization of Resistance to the Nonnucleoside NS5B Inhibitor Filibuvir in Hepatitis C Virus-Infected Patients

2011 ◽  
Vol 56 (3) ◽  
pp. 1331-1341 ◽  
Author(s):  
Philip J. F. Troke ◽  
Marilyn Lewis ◽  
Paul Simpson ◽  
Katrina Gore ◽  
Jennifer Hammond ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Amino Acid ◽  
Site Directed Mutagenesis ◽  
Phenotypic Resistance ◽  
Number Of Patients ◽  
Chronic Hcv ◽  
Selection Of

ABSTRACTFilibuvir (PF-00868554) is an investigational nonnucleoside inhibitor of the hepatitis C virus (HCV) nonstructural 5B (NS5B) RNA-dependent RNA polymerase currently in development for treating chronic HCV infection. The aim of this study was to characterize the selection of filibuvir-resistant variants in HCV-infected individuals receiving filibuvir as short (3- to 10-day) monotherapy. We identified amino acid M423 as the primary site of mutation arising upon filibuvir dosing. Through bulk cloning of clinical NS5B sequences into a transient-replicon system, and supported by site-directed mutagenesis of the Con1 replicon, we confirmed that mutations M423I/T/V mediate phenotypic resistance. Selection in patients of an NS5B mutation at M423 was associated with a reduced replicative capacityin vitrorelative to the pretherapy sequence; consistent with this, reversion to wild-type M423 was observed in the majority of patients following therapy cessation. Mutations at NS5B residues R422 and M426 were detected in a small number of patients at baseline or the end of therapy and also mediate reductions in filibuvir susceptibility, suggesting these are rare but clinically relevant alternative resistance pathways. Amino acid variants at position M423 in HCV NS5B polymerase are the preferred pathway for selection of viral resistance to filibuvirin vivo.

scholarly journals Potential Selection of LMP1 Variants in Nasopharyngeal Carcinoma

2004 ◽  
Vol 78 (2) ◽  
pp. 868-881 ◽  
Author(s):  
Rachel H. Edwards ◽  
Diane Sitki-Green ◽  
Dominic T. Moore ◽  
Nancy Raab-Traub
Keyword(s):  
Amino Acid ◽  
Cytotoxic T Lymphocyte ◽  
Amino Acid Sequences ◽  
Barr Virus ◽  
Distinct Sequence ◽  
Epstein Barr ◽  
Virus Latent Membrane Protein ◽  
Multiple Strains ◽  
Carboxy Terminal ◽  
Selection Of

ABSTRACT Seven distinct sequence variants of the Epstein-Barr virus latent membrane protein 1 (LMP1) have been identified by distinguishing amino acid changes in the carboxy-terminal domain. In this study the transmembrane domains are shown to segregate identically with the distinct carboxy-terminal amino acid sequences. Since strains of LMP1 have been shown to differ in abundance between blood and throat washes, nasopharyngeal carcinomas (NPCs) from areas of endemicity and nonendemicity with matching blood were analyzed by using a heteroduplex tracking assay to distinguish LMP1 variants. Striking differences were found between the compartments with the Ch1 strain prevalent in the NPCs from areas of endemicity and nonendemicity and the B958 strain prevalent in the blood of the endemic samples, whereas multiple strains of LMP1 were prevalent in the blood of the nonendemic samples. The possible selection against the B958 strain appearing in the tumor was highly significant (P < 0.0001). Sequence analysis of the full-length LMP1 variants revealed changes in many of the known and computer-predicted HLA-restricted epitopes with changes in key positions in multiple, potential epitopes for the specific HLA of the patients. These amino acid substitutions at key positions in the LMP1 epitopes may result in a reduced cytotoxic-T-lymphocyte response. These data indicate that strains with specific variants of LMP1 are more likely to be found in NPC. The predominance of specific LMP1 variants in NPC could reflect differences in the biologic or molecular properties of the distinct forms of LMP1 or possible immune selection.

Somatotropin increases protein balance independent of insulin's effects on protein metabolism in growing pigs

2000 ◽  
Vol 279 (1) ◽  
pp. E1-E10 ◽  
Author(s):  
Rhonda C. Vann ◽  
Hanh V. Nguyen ◽  
Peter J. Reeds ◽  
Norman C. Steele ◽  
Daniel R. Deaver ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Metabolism ◽  
Growing Pigs ◽  
Whole Body ◽  
Metabolic Responses ◽  
Glucose Disposal ◽  
Blood Levels ◽  
Protein Balance ◽  
Protein Deposition ◽  
Leucine Oxidation

Somatotropin (ST) administration enhances protein deposition and elicits profound metabolic responses, including hyperinsulinemia. To determine whether the anabolic effect of ST is due to hyperinsulinemia, pair-fed weight-matched growing swine were treated with porcine ST (150 μg · kg body wt−1 · day−1) or diluent for 7 days ( n = 6/group, ∼20 kg). Then pancreatic glucose-amino acid clamps were performed after an overnight fast. The objective was to reproduce the insulin levels of 1) fasted control and ST pigs (basal insulin, 5 μU/ml), 2) fed control pigs (low insulin, 20 μU/ml), and 3) fed ST pigs (high insulin, 50 μU/ml). Amino acid and glucose disposal rates were determined from the infusion rates necessary to maintain preclamp blood levels of these substrates. Whole body nonoxidative leucine disposal (NOLD), leucine appearance (Ra), and leucine oxidation were determined with primed, continuous infusions of [13C]leucine and [14C]bicarbonate. ST treatment was associated with higher NOLD and protein balance and lower leucine oxidation and amino acid and glucose disposals. Insulin lowered Ra and increased leucine oxidation, protein balance, and amino acid and glucose disposals. These effects of insulin were suppressed by ST treatment; however, the protein balance remained higher in ST pigs. The results show that ST treatment inhibits insulin's effects on protein metabolism and indicate that the stimulation of protein deposition by ST treatment is not mediated by insulin. Comparison of the protein metabolic responses to ST treatment during the basal fasting period with those in the fully fed state from a previous study suggests that the mechanism by which ST treatment enhances protein deposition is influenced by feeding status.

scholarly journals Nutritional and energetic value of rice by-products, with or without phytase, for growing pigs

2015 ◽  
Vol 45 (7) ◽  
pp. 1305-1310
Author(s):  
Julio Cezar Dadalt ◽  
Andréa Machado Leal Ribeiro ◽  
Alexandre de Mello Kessler ◽  
William Rui Wesendonck ◽  
Luciane Bockor ◽  
...  
Keyword(s):  
Rice Bran ◽  
Control Diet ◽  
Sampling Period ◽  
Protein Digestibility ◽  
Growing Pigs ◽  
Metabolizable Energy ◽  
Defatted Rice Bran ◽  
P Utilization ◽  
Digestible Protein ◽  
By Products

The objective of this study was to evaluate nutritional and energetic value of rice by-products, with or without phytase, using growing pigs. Thirty-six male pigs were housed in individual metabolic cages. Total collection of feces and urine was carried out in two periods of ten days: five days for adaptation and five days for collection. A randomized blocks design was used, considering the sampling period as a block, with five treatments and seven replicates. Two control diets (with and without phytase - Phy) were used in the digestibility calculations, the latter in order to evaluate the enzyme influence on energy digestibility of the tested ingredients. The control diet was replaced by 30% of one of the ingredients: defatted rice bran (DRB) with and without Phy and dephytinised defatted rice bran (DDRB). The use of Phy in the control diet did not influence DRB+Phy energy digestibility. Relative to DRB+Phy, dephytinised defatted rice bran had higher contents of ME and digestible protein but lower digestible P and Ca. Phy supplementation increased Ca and P utilization of DRB and improved energy and protein digestibility. The DRB without Phy showed the lowest digestibility coefficients for all responses. Metabolizable energy, digestible protein, phosphorus and calcium of DRB, DRB+Phy and DDRB were respectively, 2140, 2288 and 2519kcal kg-1; 79.25, 92.41 and 107.10g kg-1; 1.62, 3.41, and 2.11g kg-1 and 2.80, 3.79 and 2.90g kg-1.

Directed selection of amino acid changes in the influenza hemagglutinin and neuraminidase affecting protein antigenicity

Vaccine ◽  
2018 ◽  
Vol 36 (43) ◽  
pp. 6383-6392 ◽  
Author(s):  
Marta L. DeDiego ◽  
Kevin Chiem ◽  
David J. Topham
Keyword(s):  
Amino Acid ◽  
Influenza Hemagglutinin ◽  
Selection Of
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