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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/8809
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dc.contributor.authorPalaiomylitou, M. A.en
dc.contributor.authorKalimanis, A.en
dc.contributor.authorKoukkou, A. I.en
dc.contributor.authorDrainas, C.en
dc.contributor.authorAnastassopoulos, E.en
dc.contributor.authorPanopoulos, N. J.en
dc.contributor.authorEkateriniadou, L. V.en
dc.contributor.authorKyriakidis, D. A.en
dc.date.accessioned2015-11-24T16:44:30Z-
dc.date.available2015-11-24T16:44:30Z-
dc.identifier.issn0011-2240-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8809-
dc.rightsDefault Licence-
dc.subjectice nucleation proteinen
dc.subjectinaz geneen
dc.subjecte-colien
dc.subjectreconstitutionen
dc.subjectexpressionen
dc.subjectidentificationen
dc.subjectpurificationen
dc.subjectmutagenesisen
dc.subjectproducten
dc.subjectinvitroen
dc.subjectnucleien
dc.subjectlipidsen
dc.titlePhospholipid analysis and fractional reconstitution of the ice nucleation protein activity purified from Escherichia coli overexpressing the inaZ gene of Pseudomonas syringaeen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDOI 10.1006/cryo.1998.2102-
heal.identifier.secondary<Go to ISI>://000075366600008-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0011224098921022/1-s2.0-S0011224098921022-main.pdf?_tid=5c63a2ae-357f-11e3-a3cd-00000aacb361&acdnat=1381830867_16c67e1569a22455796e1228af5332c9-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1998-
heal.abstractIce nucleation protein was partially purified from the membrane fraction of E. coli carrying inaZ from Pseudomonas syringae. The ice nucleation protein was totally localized in the bacterial envelope and was extracted by either salt (0.25 M NH4Cl) or the nonionic detergent Tween 20. The extracted protein was partially purified by sequential passage through DEAE-52 cellulose and Sephacryl-S400 columns. The activity of the purified protein was lost after treatment with phospholipase C, and its activity was subsequently restored by addition of the naturally occurring Lipid phosphatidylethanolamine. These results suggest that ice nucleation proteins have a requirement for lipids that reconstitute a physiological hydrophobic environment similar to the one existing in vivo, to attain and maintain a structure that enables ice catalysis. (C) 1998 Academic Press.en
heal.publisherElsevieren
heal.journalNameCryobiologyen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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