1,271 research outputs found

    Pressure-induced structural, electronic, and magnetic effects in BiFeO3

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    We present a first-principles study of multiferroic BiFeO3 at high pressures. Our work reveals the main structural (change in Bi's coordination and loss of ferroelectricity), electronic (spin crossover and metallization), and magnetic (loss of order) effects favored by compression and how they are connected. Our results are consistent with the striking manifold transition observed experimentally by Gavriliuk et al. [Phys. Rev. B 77, 155112 (2008)] and provide an explanation for it.Comment: 4 pages with 4 figures embedded. More information at http://www.icmab.es/dmmis/leem/jorg

    Characterization of fimbriae extracts from porcine enterotoxigenic Escherichia coli strains carrying F6 (987P) antigen

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    Fimbrial extracts from porcine enterotoxigenic Escherichia coli (ETEC) strains carrying F6 (987P) intestinal colonization factor antigen were obtained using the thermal shock method. The extracts were analyzed by SDSPAGE and immunoblotting using different fimbriae-specific antisera. Two major protein bands with molecular masses of 17.5 and 21.9 kDa were detected. The 21.9-kDa band was identified as the major subunit of F6 fimbrial antigen in strains of serogroups O9 and O141. The 17.5-kDa band was associated with porcine strains of serogroups O9 and O20. [Int Microbiol 2006; 9(4):241-246

    High pressure effects on the activities of cathepsins B and D of mackerel and horse mackerel muscle

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    We determined high pressure processing (HPP) effects on the activities of cathepsins B and D in the muscles of mackerel (Scomber scombrus) and horse mackerel (Trachurus trachurus). In mackerel, the cathepsin B activity decrease reached 40% at 450 MPa while in horse mackerel, low and intermediate pressures (150 and 300 MPa) caused an activity increase (30%) but at 450 MPa a decrease of up to 60%. In both species, cathepsin D activity increased after a 300 MPa treatment (up to 2-fold for mackerel and 60% for horse mackerel) and decreased on a 450 MPa treatment. The activity increase is probably due to HPP damage of lysosome releasing enzymes into the fish muscle. Based on the HPP effects on the activities of cathepsins B and D, 450 MPa may be used to reduce the proteolytic activity of cathepsin B prior to chilled or frozen storage of these fish speciesSupported by the Xunta de Galicia, Spain Project 10TAL402001PR, 2010-2012, and FCT (Portugal), European Union, QREN, FEDER and COMPETE thorough QOPNA research unit, Project PEst-C/QUI/UI0062/2013; FCOMP-01-0124-FEDER-037296. Also supported by he USDA National Institute of Food and Agriculture, Grants No. 2011-31200-06041 and 2012-31200-06041S
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