1000 resultados para Dionysius, of Halicarnassus


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Mode of access: Internet.

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O estilo de Tucídides foi estudado desde a Antiguidade, sendo a obra mais completa, apesar de não elogiosa, a de Dionísio de Halicarnasso. Este artigo foca alguns dos elementos mais característicos da escrita de Tucídides, estruturando-os em pequenas secções que abrangem a «variatio», os paralelismos, os «hapax legomena», as abstrações, as definições de conceitos, as generalizações e o uso de documentos «verbatim».

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Includes The Life of Homer, attributed to Herodotus of Halicarnassus. Translated by Kenneth R. H. Mackenzie. Pages v-xxxii .

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Added title page in English: The history of Herodotus of Halicarnassus in nine books.

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Mode of access: Internet.

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"The plates are from drawings made by Corporal R. Spackman, R.E. (British Museum Add. Ms. 30, 988) ..."

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A wide range of peptides produced from milk proteins have been demonstrated to produce a physiological response in model systems. These peptides may be released from intact proteins in the gastrointestinal tract by proteolytic digestion, but are also present in fermented products such as cheese and yogurt, as a result of the action of inherent proteases, such as plasmin, and/or bacterial proteases released by the starter culture. This study investigated the presence of peptides, previously reported to have bioactive properties, in commercially available yogurts and cheeses.

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Several peptides sharing high sequence homology with lactoferricin B (Lf-cin B) were generated from bovine lactoferrin (Lf) with recombinant chymosin. Two peptides were copurified. one identical to Lf-cin B and another differing from Lf-cin B by the inclusion of a C-terminal alanine (lactoferricin). Two other peptides were copurified from chymosin-hydrolyzed Lf. one differing from Lf-cin B by the inclusion of C-terminal alanyl-leucine and the other being a heterodimer linked by a disulfide bond, These peptides were isolated in a single step from chymosin-hydrolyzed Lf by membrane ton-exchange chromatography and were purified by reverse-phase high-pressure liquid chromatography (HPLC), They were characterized by. N-terminal Edman sequencing, mass spectrometry, and antibacterial activity determination, Pure lactoferricin, prepared from pepsin-hydrolyzed Lf, was purified by standard chromatography techniques, This peptide was analyzed against a number of gram-positive and gram-negative bacteria before and after reduction of its disulfide bond or cleavage after its single methionine residue and was found to inhibit the growth of all the test bacteria at a concentration of 8 mu M or less, Subfragments of lactoferricin were isolated from reduced and cleaved peptide by reverse-phase HPLC, Subfragment 1 (residues I to 10) was active against most of the test microorganisms at concentrations of 10 to 50 mu M. Subfragment 2 (residues 11 to 26) was active against only a few microorganisms at concentrations up to 100 mu M. These antibacterial studies indicate that the activity of lactoferricin Is mainly, but not wholly, due to its N-terminal region.