920 resultados para Oriental philology.


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http://www.archive.org/details/anorientallandof00freeuoft

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This file contains a finding aid for the Bulletin of the American Schools of Oriental Research (BASOR) Collection. To access the collection, please contact the archivist (asorarch@bu.edu) at the American Schools of Oriental Research, located at Boston University.

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Se incluyen en este trabajo 40 taxones recolectados en la Sierra de Quintana (provincia de Jaén); la mayor parte de ellos constituyen novedades para la flora de esta provincia. Algunos se citan por primera vez para Andalucía oriental: Illecebrum verticillatum L., Cicendia filiformis (L.) Delarbre, Exaculum pusillum (Lam.) Carnel in Parl., Gratiola linifolia Vahl., Laurentia gasparrini (Tineo) Strobl., etc.

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Se comentan 14 taxones raros o no conocidos hasta ahora en Andalucía Oriental; para cada especie se aportan datos ecológicos, fitosociológicos y corológicos y en algunos casos también de tipo nomenclatural.

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Se proponen dos nuevas asociaciones de pastizales presentes en las montañas de Andalucía oriental: Brachypodio boissieri-Trisetetum velutini y Seseli granatensis-Festucetum hystricis. Así mismo se da cuenta de la ecología, corología y sinfitosociología de ambos sintáxones.

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Se comenta el comportamiento ecológico y corologia de veinte táxones de Andalucia oriental poco o nada conocidos, de los que destacamos: Geum rivale L., Convolvulus cantabricus L., Scrophularia frutescens L., Plantago loeflingii L., Koeleria caudata (Link) Steudel y K. dasyphylla Willk.

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The structural diversity of polypeptides in amphibian skin secretion probably reflects different roles in dermal regulation or in defense against predators. Here we report the structures of two novel trypsin inhibitor analogs, BOTI and BVTI, from the dermal venom of the toads, Bombina orientalis and Bombina variegata. Cloning of their respective precursors was achieved from lyophilized venom cDNA libraries for the first time. Amino acid alignment revealed that both deduced peptides, consisting of 60 amino acid residues, including 10 cysteines and the reactive center motif, -CDKKC-, can be affirmed as structural homologs of the trypsin inhibitor from Bombina bombina skin.

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Amphibian skin secretions contain a broad spectrum of biologically active compounds, particularly antimicrobial peptides, which are considered to constitute a first line of defence against bacterial infection. Here we describe the identification of two prototype peptides representing a novel structural class of antimicrobial peptide from the skin secretion of the oriental broad-folded frog, Hylarana latouchii. Named hylaranin-L1 (GVLSAFKNALPGIMKIIVamide) and hylaranin-L2 (GVLSVIKNALPGIMRFIAamide), both peptides consist of 18 amino acid residues, are C-terminally amidated and are of unique primary structures. Their primary structures were initially deduced by MS/MS fragmentation sequencing from reverse-phase HPLC fractions of skin secretion that demonstrated antimicrobial activity. Subsequently, their precursor-encoding cDNAs were cloned from a skin secretion-derived cDNA library and their primary structures were confirmed unequivocally. Synthetic replicates of both peptides exhibited broad-spectrum antimicrobial activity with mean inhibitory concentrations (MICs) of 34 µM against Gram-negative Escherichia coli, 4.3 µM against Gram-positive Staphylococcus aureus and 4–9 µM against the yeast, Candida albicans. Both peptides exhibited little haemolytic activity (<6 %) at the MICs for S. aureus and C. albicans. Amphibian skin secretions thus continue to provide novel antimicrobial peptide structures that may prove to be lead compounds in the design of new classes of anti-infection therapeutics.