10 resultados para AB01


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We have developed a new technique for quantifying methionine sulfoxide (MetSO) in protein to assess levels of oxidative stress in physiological systems. In this procedure, samples are hydrolyzed with methanesulfonic acid (MSA) in order to avoid the conversion of MetSO to methionine (Met) that occurs during hydrolysis of protein in HCl. The hydrolysate is fractionated on a cation exchange column to remove the nonvolatile MSA from amino acids, and the amino acids are then derivatized as their trimethylsilyl esters for analysis by selected ion monitoring-gas chromatography/mass spectrometry. The limit of detection of the assay is 200 pmol of MetSO per analysis, and the interassay coefficient of variation is 5.8%. Compared to current methods, the SIM-GC/MS assay avoids the potential for conversion of Met to MetSO during sample preparation, requires less sample preparation time, has lower variability, and uses mass spectrometry for sensitive and specific analyte detection.

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Three groups of cows representing three ranges of welfare in the production system were included in the study: two groups of Bruna dels Pirineus beef cattle maintained under different management systems (good and semiferal conditions) and a group of Alberes cows, a breed that lives in the mountains (hardest conditions).

In order to identify new stress/welfare biomarkers, serum from Bruna cows living in both environments was subjected to DIGE labelling, two-dimensional electrophoresis and MALDI-MS or ion trap MS. Identification was achieved for 15 proteins, which mainly belonged to three biological functions, the oxidative stress pathway (glutathione peroxidase (GPx) and paraoxonase (PON-1)), the acute phase protein family (Heremans Schmid glycoprotein alpha2 (α2-HSG)) and the complement system.

Biological validation included the Alberes breed. GPx and PON-1 were validated by an enzymatic assay and found to be higher and lower, respectively, in cows living in hard conditions. α2-HSG was validated by ELISA and found to be reduced in hard conditions. Other biomarkers of the redox status were also altered by living conditions: protein carbonyl content, superoxide dismutase (SOD) and glutathione reductase (GR).

Our results show that changes in the redox system are the main adaptation of cows living in challenging environmental conditions. This article is part of a Special Issue entitled: “Farm animal proteomics”.

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In this paper, we propose general-order transmit antenna selection to enhance the secrecy performance of multiple-input–multiple-output multieavesdropper channels with outdated channel state information (CSI) at the transmitter. To evaluate the effect of the outdated CSI on the secure transmission of the system, we investigate the secrecy performance for two practical scenarios, i.e., Scenarios I and II, where the eavesdropper's CSI is not available at the transmitter and is available at the transmitter, respectively. For Scenario I, we derive exact and asymptotic closed-form expressions for the secrecy outage probability in Nakagami- m fading channels. In addition, we also derive the probability of nonzero secrecy capacity and the \varepsilon -outage secrecy capacity, respectively. Simple asymptotic expressions for the secrecy outage probability reveal that the secrecy diversity order is reduced when the CSI is outdated at the transmitter, and it is independent of the number of antennas at each eavesdropper N_text\rm{E} , the fading parameter of the eavesdropper's channel m_text\rm{E} , and the number of eavesdroppers M . For Scenario II, we make a comprehensive analysis of the average secrecy capacity obtained by the system. Specifically, new closed-form expressions for the exact and asymptotic average secrecy capacity are derived, which are valid for general systems with an arbitrary number of antennas, number of eavesdroppers, and fading severity parameters. Resorting to these results, we also determine a high signal-to-noise ratio power offset to explicitly quantify the impact of the main c- annel and the eavesdropper's channel on the average secrecy capacity.