Effect of Energetic Supplementation on Forage Losses in an Oat and Italian Ryegrass Pasture under Continuous Grazing

The experiment was conducted at UFSM-RS to quantify herbage losses in oat and Italian ryegrass mixture under continuous grazing by beef heifers. A continuous grazing method with variable stocking rate was utilized to maintain the same herbage mass, 1500 kg DM/ha, in all treatments. The treatments consisted of levels of energetic supplement (0, 0.7 and 1.4% of LW/day). The pasture was evaluated every 28 days, when forage not suitable for grazing was collected in points previously marked in experimental area. The daily losses of herbage mass were of 22.32, 18.98 and 21.16 kg of DM/ha/day, equivalent to 2.61, 1.91 and 1.41% of LW for levels of 0, 0.7 and 1.4% of LW/day, respectively. The results showed greater stocking rates in supplemented treatments, being 21.2% and 57.4% higher in 0.7 and 1.4% LW/day, respectively, than unsupplemented one

Dynamics and Production of Forage in Winter Pasture under Continuous Grazing with Energetic Supplementation

This experiment was carried out at Federal University of Santa Maria, from July 09 to November 12, 1999 to evaluate the dynamics and production of forage of oat (Avena strigosa Schreb) and italian ryegrass (Lolium multiflorum Lam) mixture. The grazing system used was continuous with variable stocking rate to maintain 1500kg/ha of herbage mass in all treatments. The heifers were subjected to different levels of energetic supplementation. They are 0, 0.7 and 1.4% of LW/day. The pasture of oat and italian ryegrass presented an accumulation rate of 45.7, 55.1 and 50.0 kg of DM/ha /day and a total dry matter (DM) production of 7067, 7222 and 8137 kg/ha for 0, 0.7 and 1.4% of LW/day levels, respectively. The average percentage of leaf component was 8.26, 11.48 and 11.72 for oat and 23.12, 22.35 and 20.93 for Italian ryegrass at 0, 0.7 and 1.4% of LW/day levels, respectively. The supplementation neither affected the accumulation rate nor the total DM production of the pasture (P\u3e 0.05). The senescent material was lower (P\u3c 0.05) with no supplementation

Non-Commutative Gauge Theories and the Cosmological Constant

We discuss the issue of the cosmological constant in non-commutative non-supersymmetric gauge theories. In particular, in orbifold field theories non-commutativity acts as a UV cut-off. We suggest that in these theories quantum corrections give rise to a vacuum energy \rho, that is controlled by the non-commutativity parameter \theta, \rho ~ 1/theta^2 (only a soft logarithmic dependence on the Planck scale survives). We demonstrate our claim in a two-loop computation in field theory and by certain higher loop examples. Based on general expressions from string theory, we suggest that the vacuum energy is controlled by non-commutativity to all orders in perturbation theory.Comment: 11 pages, RevTex. 4 eps figures. v2: Typos corrected. To appear in Phys.Rev.

Characterization of the plasma proteome from healthy adult dogs

Introduction: Bloodwork is a widely used diagnostic tool in veterinary medicine, as diagnosis and therapeutic interventions often rely on blood biomarkers. However, biomarkers available in veterinary medicine often lack sensitivity or specificity. Mass spectrometry-based proteomics technology has been extensively used in the analysis of biological fluids. It offers excellent potential for a more comprehensive characterization of the plasma proteome in veterinary medicine. Methods: In this study, we aimed to identify and quantify plasma proteins in a cohort of healthy dogs and compare two techniques for depleting high-abundance plasma proteins to enable the detection of lower-abundance proteins via label-free quantification liquid chromatography-mass spectrometry. We utilized surplus lithium-heparin plasma from 30 healthy dogs, subdivided into five groups of pooled plasma from 6 randomly selected individuals each. Firstly, we used a commercial kit to deplete high-abundance plasma proteins. Secondly, we employed an in-house method to remove albumin using Blue-Sepharose. Results and discussion: Among all the samples, some of the most abundant proteins identified were apolipoprotein A and B, albumin, alpha-2-macroglobulin, fibrinogen beta chain, fibronectin, complement C3, serotransferrin, and coagulation factor V. However, neither of the depletion techniques achieved significant depletion of highly abundant proteins. Despite this limitation, we could detect and quantify many clinically relevant proteins. Determining the healthy canine proteome is a crucial first step in establishing a reference proteome for canine plasma. After enrichment, this reference proteome can later be utilized to identify protein markers associated with different diseases, thereby contributing to the diagnosis and prognosis of various pathologies

Characterization of the plasma proteome from healthy adult dogs

IntroductionBloodwork is a widely used diagnostic tool in veterinary medicine, as diagnosis and therapeutic interventions often rely on blood biomarkers. However, biomarkers available in veterinary medicine often lack sensitivity or specificity. Mass spectrometry-based proteomics technology has been extensively used in the analysis of biological fluids. It offers excellent potential for a more comprehensive characterization of the plasma proteome in veterinary medicine.MethodsIn this study, we aimed to identify and quantify plasma proteins in a cohort of healthy dogs and compare two techniques for depleting high-abundance plasma proteins to enable the detection of lower-abundance proteins via label-free quantification liquid chromatography-mass spectrometry. We utilized surplus lithium-heparin plasma from 30 healthy dogs, subdivided into five groups of pooled plasma from 6 randomly selected individuals each. Firstly, we used a commercial kit to deplete high-abundance plasma proteins. Secondly, we employed an in-house method to remove albumin using Blue-Sepharose.Results and discussionAmong all the samples, some of the most abundant proteins identified were apolipoprotein A and B, albumin, alpha-2-macroglobulin, fibrinogen beta chain, fibronectin, complement C3, serotransferrin, and coagulation factor V. However, neither of the depletion techniques achieved significant depletion of highly abundant proteins. Despite this limitation, we could detect and quantify many clinically relevant proteins. Determining the healthy canine proteome is a crucial first step in establishing a reference proteome for canine plasma. After enrichment, this reference proteome can later be utilized to identify protein markers associated with different diseases, thereby contributing to the diagnosis and prognosis of various pathologies