University of Oviedo

About: University of Oviedo is a education organization based out in Oviedo, Spain. It is known for research contribution in the topics: Population & Catalysis. The organization has 13423 authors who have published 31649 publications receiving 844799 citations. The organization is also known as: Universidá d'Uviéu & Universidad de Oviedo.

Purification and characterization of an extracellular protease from the fish pathogen Yersinia ruckeri and effect of culture conditions on production.

Abstract: A novel protease, hydrolyzing azocasein, was identified, purified, and characterized from the culture supernatant of the fish pathogen Yersinia ruckeri. Exoprotease production was detected at the end of the exponential growth phase and was temperature dependent. Activity was detected in peptone but not in Casamino Acid medium. Its synthesis appeared to be under catabolite repression and ammonium control. The protease was purified in a simple two-step procedure involving ammonium sulfate precipitation and ion-exchange chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the purified protein indicated an estimated molecular mass of 47 kDa. The protease had characteristics of a cold-adapted protein, i.e., it was more active in the range of 25 to 42°C and had an optimum activity at 37°C. The activation energy for the hydrolysis of azocasein was determined to be 15.53 kcal/mol, and the enzyme showed a rapid decrease in activity at 42°C. The enzyme had an optimum pH of around 8. Characterization of the protease showed that it required certain cations such as Mg2+ or Ca2+ for maximal activity and was inhibited by EDTA, 1,10-phenanthroline, and EGTA but not by phenylmethylsulfonyl fluoride. Two N-methyl-N-nitro-N-nitrosoguanidine mutants were isolated and analyzed; one did not show caseinolytic activity and lacked the 47-kDa protein, while the other was hyperproteolytic and produced increased amounts of the 47-kDa protein. Azocasein activity, SDS-PAGE, immunoblotting by using polyclonal anti-47-kDa-protease serum, and zymogram analyses showed that protease activity was present in 8 of 14 strains tested and that two Y. ruckeri groups could be established based on the presence or absence of the 47-kDa protease.

Immunization with Potato Plants Expressing VP60 Protein Protects against Rabbit Hemorrhagic Disease Virus

Abstract: The major structural protein VP60 of rabbit hemorrhagic disease virus (RHDV) has been produced in transgenic potato plants under the control of a cauliflower mosaic virus 35S promoter or a modified 35S promoter that included two copies of a strong transcriptional enhancer. Both types of promoters allowed the production of specific mRNAs and detectable levels of recombinant VP60, which were higher for the constructs carrying the modified 35S promoter. Rabbits immunized with leaf extracts from plants carrying this modified 35S promoter showed high anti-VP60 antibody titers and were fully protected against the hemorrhagic disease.

TFOS DEWS II Introduction

Abstract: J. Daniel Nelson, MD a, b, , Jennifer P. Craig, MCOptom, PhD , Esen K. Akpek MD , Dimitri T. Azar, MD , Carlos Belmonte, MD, PhD f, , Anthony J. Bron, FRCOphth, FMedSci h, , Janine A. Clayton, MD , Murat Dogru, MD, PhD k, , Harminder S. Dua, MD, PhD , Gary N. Foulks, MD , Jos e A.P. Gomes, MD, PhD , Katherine M. Hammitt, MA , Juha Holopainen, MD, PhD , Lyndon Jones, FCOptom, PhD , Choun-Ki Joo, MD, PhD , Zuguo Liu, MD, PhD , Jason J. Nichols, OD, PhD , Kelly K. Nichols, OD, PhD , Gary D. Novack, PhD v, , Virender Sangwan, MBBS, MS , Fiona Stapleton, MCOptom, PhD , Alan Tomlinson, FCOptom, DSc , Kazuo Tsubota, MD , Mark D.P. Willcox, PhD, DSc , James S. Wolffsohn, FCOptom PhD , David A. Sullivan, PhD ac

Cooperative Light-Activated Iodine and Photoredox Catalysis for the Amination of Csp3 -H Bonds.

Abstract: An unprecedented method that makes use of the cooperative interplay between molecular iodine and photoredox catalysis has been developed for dual light-activated intramolecular benzylic C-H amination Iodine serves as the catalyst for the formation of a new C-N bond by activating a remote Csp3 -H bond (1,5-HAT process) under visible-light irradiation while the organic photoredox catalyst TPT effects the reoxidation of the molecular iodine catalyst To explain the compatibility of the two involved photochemical steps, the key N-I bond activation was elucidated by computational methods The new cooperative catalysis has important implications for the combination of non-metallic main-group catalysis with photocatalysis

Strain-Tunable GaAs Quantum Dot: A Nearly Dephasing-Free Source of Entangled Photon Pairs on Demand.

Abstract: We report on the observation of nearly maximally entangled photon pairs from semiconductor quantum dots, without resorting to postselection techniques. We use GaAs quantum dots integrated on a patterned piezoelectric actuator capable of suppressing the exciton fine structure splitting. By using a resonant two-photon excitation, we coherently drive the biexciton state and demonstrate experimentally that our device generates polarization-entangled photons with a fidelity of 0.978(5) and a concurrence of 0.97(1) taking into account the nonidealities stemming from the experimental setup. By combining fine-structure-dependent fidelity measurements and a theoretical model, we identify an exciton spin-scattering process as a possible residual decoherence mechanism. We suggest that this imperfection may be overcome using a modest Purcell enhancement so as to achieve fidelities >0.99, thus making quantum dots evenly matched with the best probabilistic entangled photon sources.