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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/20571
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dc.contributor.authorEconomou, M.en
dc.contributor.authorSeferiadis, K.en
dc.contributor.authorFrangou-Lazaridis, M.en
dc.contributor.authorHorecker, B. L.en
dc.contributor.authorTsolas, O.en
dc.date.accessioned2015-11-24T19:08:42Z-
dc.date.available2015-11-24T19:08:42Z-
dc.identifier.issn0014-5793-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20571-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectChromatography, Gelen
dc.subjectChromatography, High Pressure Liquiden
dc.subjectHumansen
dc.subjectIsoelectric Focusingen
dc.subjectKidney/analysisen
dc.subjectLung/analysisen
dc.subjectMaleen
dc.subjectMolecular Sequence Dataen
dc.subjectOrgan Specificityen
dc.subjectPeptide Fragments/isolation & purificationen
dc.subject*Protein Precursors/isolation & purificationen
dc.subjectRatsen
dc.subjectSpecies Specificityen
dc.subjectSpleen/analysisen
dc.subjectSwineen
dc.subjectThymosin/*analogs & derivatives/isolation & purificationen
dc.subjectThymus Gland/analysisen
dc.subjectTrypsinen
dc.titleIsolation and partial characterization of prothymosin alpha from porcine tissuesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/3384098-
heal.identifier.secondaryhttp://ac.els-cdn.com/0014579388804563/1-s2.0-0014579388804563-main.pdf?_tid=7e1b7aa141995ed9e00b835e87e445d2&acdnat=1337335272_40c1ac9531eed4d16932b4395b766c14-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1988-
heal.abstractProthymosin alpha, an immunoactive polypeptide of 12 kDa, has been isolated from porcine thymus, spleen, lung and kidney. It lacks aromatic and sulfur-containing amino acids and has a high content of glutamic and aspartic acids. Tryptic digestion of porcine thymus prothymosin alpha yielded peptides which on separation, amino acid analysis and alignment with the known sequence of prothymosin alpha from rat and man showed that the amino terminal portion of the molecule is conserved and the few differences present are confined to the carboxy terminal.en
heal.journalNameFEBS Letten
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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