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dc.contributor.authorMallatou, H.en
dc.contributor.authorPappas, C. P.en
dc.contributor.authorAlbanis, T. A.en
dc.date.accessioned2015-11-24T16:48:30Z-
dc.date.available2015-11-24T16:48:30Z-
dc.identifier.issn0306-7319-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9331-
dc.rightsDefault Licence-
dc.subjectmethyl parathionen
dc.subjectcaseinen
dc.subjectewe's milken
dc.subjectacid-phosphataseen
dc.subjectbovine caseinen
dc.subjectdephosphorylationen
dc.titleStudy of binding of methyl parathion by cow's casein in model systems and in ewe's milken
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1080/03067310310001593693-
heal.identifier.secondary<Go to ISI>://000186506700015-
heal.identifier.secondaryhttp://www.tandfonline.com/doi/pdf/10.1080/03067310310001593693-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2004-
heal.abstractThe binding of methyl parathion by cow's casein, in model systems and in sheep's milk was investigated. Casein in cow's milk binds methyl parathion to a great extent. The addition of the enzyme potato acid phosphatase (PAP) in casein solutions does not affect the release of methyl parathion from casein. Storage of casein solutions or casein solutions plus PAP at 4degreesC for 60 days does not affect the binding of methyl parathion to casein. The data also indicate that methyl parathion binds strongly to milk proteins and/or other substances of ewe's milk.en
heal.journalNameInternational Journal of Environmental Analytical Chemistryen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

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