{"id":{"repo_id":"greece","oai_identifier":"oai:10442/1437"},"canonical_url":"https://search.dev.ndltd.org/etd/greece/oai:10442/1437","repository":{"repo_id":"greece","name":"Greek National Archive of PhD Theses","base_url":"https://phdtheses.ekt.gr/eadd_oai/request"},"display":{"title":"ΦΩΣΦΟΡΥΛΙΩΣΗ ΠΡΩΤΕΙΝΩΝ ΣΕ ΣΥΣΤΗΜΑ ΠΡΩΤΕΙΝΟΣΥΝΘΕΣΗΣ ΕΛΕΥΘΕΡΟ ΚΥΤΤΑΡΩΝ ΑΠΟ ΣΥΚΩΤΙΠΟΝΤΙΚΟΥ. ΚΑΘΑΡΙΣΜΟΣ ΚΑΙ ΧΑΡΑΚΤΗΡΙΣΜΟΣ ΜΙΑΣ ΝΕΑΣ ΚΙΝΑΣΗΣ ΠΡΩΤΕΙΝΩΝ ΠΟΥ ΡΥΘΜΙΖΕΤΑΙ ΑΠΟ ΚΥΚΛΙΚΑ ΝΟΥΚΛΕΟΤΙΔΙΑ","abstract":"IN THE FIRST PART OF THE THESIS AN INVESTIGATION ON THE PHOSPHORYLATION OF THE PROTEIN COMPONENTS OF A CELL FREE SYSTEM OF PROTEIN SYNTHESIS OF MOUSE LIVER (POLYSOMES,\"PH5\" FRACTION) AS WELL AS THE EFFECT OF VARIOUS AGENTS ON PROTEIN PHOSPHORYLATION IS REPORTED. THE ENZYME IS A SERINE- THREONINE KINASE WITH A MOLECULAR MASS OF 90 KDA. IT CONTAINS A 47 KDA AUTOPHOSPHORYLATABLE PEPTIDE AND CONSEQUENTLY IN ALL PROBABILITY THE NATIVE ENZYME IS A HOMODIMER. IT ACTS OPTIMALLYAT PH 7.5 AND PHOSPHORYLATES HISTONES AND POLYSOMAL PROTEINS BUT NOT PROTAMINE, CASEIN OR ANY OF THE PROTEINS OF THE \"PH5\" FRACTION. AT HIGH (10- 5 M) ATP CONCENTRATIONS MG2+ IS THE MOST EFFICIENT ACTIVATING METAL WHILE AT LOW (10-9 M) ATP CONCENTRATIONS MN2+ IS. THE ACTIVITY OF THE PURIFIED KINASE IS AFFECTED BY THE PRESENCE OF ANY OF THE FOUR 3', 5' CYCLIC NUCLEOTIDES. THIS EFFECT WHICH MAY BE EITHER STIMULATORY OR INHIBITORY, DEPENDS ON THE CONCENTRATION OF ATP, ON THE TYPE OF ACTIVATING METAL EMPLOYED AS WELL AS ON THE SUBSTRATE USED. ON THE BASIS OF THE AFOREMENTIONED EFFECTS OF THE 3', 5' CYCLIC NUCLEOTIDES AND THE FACT THAT THE NATIVE ENZYME IS NOT DISSOCIATED INTO REGULATORY AND CATALYTIC SUBUNITS, THIS NOVEL KINASE NAMED CYCLIC NUCLEOTIDE- REGULATED PROTEIN KINASE (NRPK).","abstract_html":"IN THE FIRST PART OF THE THESIS AN INVESTIGATION ON THE PHOSPHORYLATION OF THE PROTEIN COMPONENTS OF A CELL FREE SYSTEM OF PROTEIN SYNTHESIS OF MOUSE LIVER (POLYSOMES,"PH5" FRACTION) AS WELL AS THE EFFECT OF VARIOUS AGENTS ON PROTEIN PHOSPHORYLATION IS REPORTED. THE ENZYME IS A SERINE- THREONINE KINASE WITH A MOLECULAR MASS OF 90 KDA. IT CONTAINS A 47 KDA AUTOPHOSPHORYLATABLE PEPTIDE AND CONSEQUENTLY IN ALL PROBABILITY THE NATIVE ENZYME IS A HOMODIMER. IT ACTS OPTIMALLYAT PH 7.5 AND PHOSPHORYLATES HISTONES AND POLYSOMAL PROTEINS BUT NOT PROTAMINE, CASEIN OR ANY OF THE PROTEINS OF THE "PH5" FRACTION. AT HIGH (10- 5 M) ATP CONCENTRATIONS MG2+ IS THE MOST EFFICIENT ACTIVATING METAL WHILE AT LOW (10-9 M) ATP CONCENTRATIONS MN2+ IS. THE ACTIVITY OF THE PURIFIED KINASE IS AFFECTED BY THE PRESENCE OF ANY OF THE FOUR 3', 5' CYCLIC NUCLEOTIDES. THIS EFFECT WHICH MAY BE EITHER STIMULATORY OR INHIBITORY, DEPENDS ON THE CONCENTRATION OF ATP, ON THE TYPE OF ACTIVATING METAL EMPLOYED AS WELL AS ON THE SUBSTRATE USED. ON THE BASIS OF THE AFOREMENTIONED EFFECTS OF THE 3', 5' CYCLIC NUCLEOTIDES AND THE FACT THAT THE NATIVE ENZYME IS NOT DISSOCIATED INTO REGULATORY AND CATALYTIC SUBUNITS, THIS NOVEL KINASE NAMED CYCLIC NUCLEOTIDE- REGULATED PROTEIN KINASE (NRPK).","abstract_has_math":false,"creators":["Nikolakaki, Eleni","Νικολακάκη, Ελένη"],"institution":"Aristotle University Of Thessaloniki (AUTH)","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1990,"date_issued":"1990","date_published":"1990","updated_at":"2026-07-24T02:24:56Z","subjects":["3', 5' CYCLIC NUCLEOTIDES","3', 5' ΚΥΚΛΙΚΑ ΝΟΥΚΛΕΟΤΙΔΙΑ","MOUSE LIVER","Protein kinases","Protein phosphorylation","Ribosomal proteins","ΚΙΝΑΣΗ ΠΡΩΤΕΙΝΩΝ","Ριβοσωμικές πρωτεΐνες","ΣΥΚΩΤΙ ΠΟΝΤΙΚΟΥ","Φωσφορυλίωση πρωτεινών","Φυσικές Επιστήμες","Χημεία","Natural Sciences","Chemical Sciences"],"languages":["gre"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["10.12681/eadd/1437"],"render_values":[{"text":"10.12681/eadd/1437","href":"https://doi.org/10.12681/eadd/1437","code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10442/hedi/1437","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Nikolakaki, Eleni","Νικολακάκη, Ελένη"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["1990"]},{"key":"dc:publisher","label":"Institution","values":["Aristotle University Of Thessaloniki (AUTH)","Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ)"]},{"key":"dc:type","label":"Dc Type","values":["PhD Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["3', 5' CYCLIC NUCLEOTIDES","3', 5' ΚΥΚΛΙΚΑ ΝΟΥΚΛΕΟΤΙΔΙΑ","MOUSE LIVER","Protein kinases","Protein phosphorylation","Ribosomal proteins","ΚΙΝΑΣΗ ΠΡΩΤΕΙΝΩΝ","Ριβοσωμικές πρωτεΐνες","ΣΥΚΩΤΙ ΠΟΝΤΙΚΟΥ","Φωσφορυλίωση πρωτεινών","Φυσικές Επιστήμες","Χημεία","Natural Sciences","Chemical Sciences"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["gre"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["10.12681/eadd/1437","http://hdl.handle.net/10442/hedi/1437"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["IN THE FIRST PART OF THE THESIS AN INVESTIGATION ON THE PHOSPHORYLATION OF THE PROTEIN COMPONENTS OF A CELL FREE SYSTEM OF PROTEIN SYNTHESIS OF MOUSE LIVER (POLYSOMES,\"PH5\" FRACTION) AS WELL AS THE EFFECT OF VARIOUS AGENTS ON PROTEIN PHOSPHORYLATION IS REPORTED. THE ENZYME IS A SERINE- THREONINE KINASE WITH A MOLECULAR MASS OF 90 KDA. IT CONTAINS A 47 KDA AUTOPHOSPHORYLATABLE PEPTIDE AND CONSEQUENTLY IN ALL PROBABILITY THE NATIVE ENZYME IS A HOMODIMER. IT ACTS OPTIMALLYAT PH 7.5 AND PHOSPHORYLATES HISTONES AND POLYSOMAL PROTEINS BUT NOT PROTAMINE, CASEIN OR ANY OF THE PROTEINS OF THE \"PH5\" FRACTION. AT HIGH (10- 5 M) ATP CONCENTRATIONS MG2+ IS THE MOST EFFICIENT ACTIVATING METAL WHILE AT LOW (10-9 M) ATP CONCENTRATIONS MN2+ IS. THE ACTIVITY OF THE PURIFIED KINASE IS AFFECTED BY THE PRESENCE OF ANY OF THE FOUR 3', 5' CYCLIC NUCLEOTIDES. THIS EFFECT WHICH MAY BE EITHER STIMULATORY OR INHIBITORY, DEPENDS ON THE CONCENTRATION OF ATP, ON THE TYPE OF ACTIVATING METAL EMPLOYED AS WELL AS ON THE SUBSTRATE USED. ON THE BASIS OF THE AFOREMENTIONED EFFECTS OF THE 3', 5' CYCLIC NUCLEOTIDES AND THE FACT THAT THE NATIVE ENZYME IS NOT DISSOCIATED INTO REGULATORY AND CATALYTIC SUBUNITS, THIS NOVEL KINASE NAMED CYCLIC NUCLEOTIDE- REGULATED PROTEIN KINASE (NRPK).","ΣΤΟ ΠΡΩΤΟ ΜΕΡΟΣ ΤΗΣ ΔΙΑΤΡΙΒΗΣ ΔΙΕΡΕΥΝΗΘΗΚΕ Η ΦΩΣΦΟΡΥΛΙΩΣΗ ΤΩΝ ΕΠΙΜΕΡΟΥΣ ΠΡΩΤΕΙΝΙΚΩΝ ΣΥΣΤΑΤΙΚΩΝ ΕΝΟΣ ΣΥΣΤΗΜΑΤΟΣ ΠΡΩΤΕΙΝΟΣΥΝΘΕΣΗΣ ΕΛΕΥΘΕΡΟΥ ΚΥΤΤΑΡΩΝ (ΠΟΛΥΣΩΜΑΤΑ, ΚΛΑΣΜΑ \"PH5\") ΑΠΟ ΣΥΚΩΤΙ ΠΟΝΤΙΚΟΥ ΚΑΘΩΣ ΚΑΙ Η ΕΠΙΔΡΑΣΗ ΔΙΑΦΟΡΩΝ ΠΑΡΑΓΟΝΤΩΝ ΠΟΥ ΤΗΝ ΕΠΗΡΕΑΖΟΥΝ. ΣΤΟ ΔΕΥΤΕΡΟ ΜΕΡΟΣ ΤΗΣ ΔΙΑΤΡΙΒΗΣ ΑΠΟΜΟΝΩΘΗΚΕ ΚΑΙ ΜΕΛΕΤΗΘΗΚΕ ΜΙΑ ΝΕΑ ΚΙΝΑΣΗ ΠΡΩΤΕΙΝΩΝ ΑΠΟ ΤΟ ΚΥΤΤΑΡΟΠΛΑΣΜΑ ΚΑΙ ΣΥΓΚΕΚΡΙΜΕΝΑ ΑΠΟ ΤΟ ΚΛΑΣΜΑ \"PH5\". Η ΚΙΝΑΣΗ ΑΥΤΗ ΤΩΝ ΠΡΩΤΕΙΝΩΝ ΕΙΝΑΙ ΚΙΝΑΣΗ ΣΕΡΙΝΗΣ- ΘΡΕΟΝΙΝΗΣ ΚΑΙ ΕΧΕΙ ΜΟΡΙΑΚΟΒΑΡΟΣ 90 KDA. ΠΕΡΙΕΧΕΙ ΜΙΑ ΑΥΤΟΦΩΣΦΟΡΥΛΙΟΥΜΕΝΗ ΥΠΟΜΟΝΑΔΑ ΤΩΝ 47 KDA ΚΑΙ ΓΙΑ ΤΟΛΟΓΟ ΑΥΤΟ ΚΑΤΑ ΠΑΣΑ ΠΙΘΑΝΟΤΗΤΑ ΤΟ ΔΡΑΣΤΙΚΟ ΕΝΖΥΜΟ ΕΙΝΑΙ ΕΝΑ ΟΜΟΔΙΜΕΡΕΣ. ΕΧΕΙ ΒΕΛΤΙΣΤΟ PH ΔΡΑΣΗΣ 7.5 ΚΑΙ ΦΩΣΦΟΡΥΛΙΩΝΕΙ ΙΣΤΟΝΕΣ ΚΑΙ ΡΙΒΟΣΗΜΙΚΕΣ ΠΡΩΤΕΙΝΕΣ ΑΛΛΑ ΟΧΙ ΚΑΖΕΙΝΗ, ΠΡΟΤΑΜΙΝΗ ΚΑΙ ΠΡΩΤΕΙΝΕΣ ΤΟΥ ΚΛΑΣΜΑΤΟΣ \"PH5\". ΣΕ ΨΗΛΕΣ ΣΥΓΚΕΝΤΡΩΣΕΙΣ ATP (10-5 Μ)ΔΡΑ ΚΑΛΥΤΕΡΑ ΠΑΡΟΥΣΙΑ MG2+, ΕΝΩ ΑΝΤΙΘΕΤΑ ΣΕ ΧΑΜΗΛΕΣ ΣΥΓΚΕΝΤΡΩΣΕΙΣATP (10-9 Μ) ΠΑΡΟΥΣΙΑ MN2+. Η ΔΡΑΣΗ ΤΗΣ ΚΙΝΑΣΗΣ ΕΠΗΡΕΑΖΕΤΑΙ ΑΠΟ ΤΗΝ ΠΑΡΟΥΣΙΑ ΤΩΝ 3', 5' ΚΥΚΛΙΚΩΝ ΝΟΥΚΛΕΟΤΙΔΙΩΝ ΚΑΙ ΤΟ ΑΠΟΤΕΛΕΣΜΑ ΕΞΑΡΤΑΤΑΙ ΤΟΣΟ ΑΠΟ ΤΗ ΣΥΓΚΕΝΤΡΩΣΗ ΤΟΥ ATP, ΟΣΟ ΚΑΙ ΑΠΟ ΤΟ ΜΕΤΑΛΛΟ ΠΟΥ ΧΡΗΣΙΜΟΠΟΙΕΙΤΑΙ ΩΣ ΕΝΕΡΓΟΠΟΙΗΤΗΣ ΚΑΘΩΣ ΚΑΙ ΑΠΟ ΤΗ ΦΥΣΗ ΤΟΥ ΥΠΟΣΤΡΩΜΑΤΟΣ. ΜΕ ΒΑΣΗ ΤΙΣ ΠΙΟ ΠΑΝΩ ΕΠΙΠΤΩΣΕΙΣ ΤΩΝ 3', 5' ΚΥΚΛΙΚΩΝ ΝΟΥΚΛΕΟΤΙΔΙΩΝ ΣΤΗ ΔΡΑΣΗ ΤΟΥ ΕΝΖΥΜΟΥ ΚΑΘΩΣ ΚΑΙ ΑΠΟ ΤΟ ΓΕΓΟΝΟΣ ΟΤΙ ΔΕΝ ΔΙΑΣΠΑΤΑΙ ΣΕ ΚΑΤΑΛΥΤΙΚΗ ΚΑΙ ΡΥΘΜΙΣΤΙΚΗ ΥΠΟΜΟΝΑΔΑ Η ΚΙΝΑΣΗ ΑΥΤΗ ΟΝΟΜΑΣΤΗΚΕ : ΚΙΝΑΣΗ ΠΟΥ Η ΔΡΑΣΗ ΤΗΣ ΡΥΘΜΙΖΕΤΑΙ ΑΠΟ ΚΥΚΛΙΚΑ ΝΟΥΚΛΕΟΤΙΔΙΑ (DNRPK, CYCLIC NUCLETIDE-REGULATED PROTEIN KINASE)."]},{"key":"dc:title","label":"Title","values":["ΦΩΣΦΟΡΥΛΙΩΣΗ ΠΡΩΤΕΙΝΩΝ ΣΕ ΣΥΣΤΗΜΑ ΠΡΩΤΕΙΝΟΣΥΝΘΕΣΗΣ ΕΛΕΥΘΕΡΟ ΚΥΤΤΑΡΩΝ ΑΠΟ ΣΥΚΩΤΙΠΟΝΤΙΚΟΥ. ΚΑΘΑΡΙΣΜΟΣ ΚΑΙ ΧΑΡΑΚΤΗΡΙΣΜΟΣ ΜΙΑΣ ΝΕΑΣ ΚΙΝΑΣΗΣ ΠΡΩΤΕΙΝΩΝ ΠΟΥ ΡΥΘΜΙΖΕΤΑΙ ΑΠΟ ΚΥΚΛΙΚΑ ΝΟΥΚΛΕΟΤΙΔΙΑ","PROTEIN PHOSPHORYLATION IN A CELL FREE SYSTEM OF PROTEIN SYNTHESIS FROM MOUSE LIVER. PURIFICATION AND CHARACTERIZATION OF A NOVEL PROTEIN KINASE REGULATED BY CYCLIC NUCLEOTIDES"]}]}],"canonical_facts":{"dc:creator":["Nikolakaki, Eleni","Νικολακάκη, Ελένη"],"dc:date":["1990"],"dc:description":["IN THE FIRST PART OF THE THESIS AN INVESTIGATION ON THE PHOSPHORYLATION OF THE PROTEIN COMPONENTS OF A CELL FREE SYSTEM OF PROTEIN SYNTHESIS OF MOUSE LIVER (POLYSOMES,\"PH5\" FRACTION) AS WELL AS THE EFFECT OF VARIOUS AGENTS ON PROTEIN PHOSPHORYLATION IS REPORTED. THE ENZYME IS A SERINE- THREONINE KINASE WITH A MOLECULAR MASS OF 90 KDA. IT CONTAINS A 47 KDA AUTOPHOSPHORYLATABLE PEPTIDE AND CONSEQUENTLY IN ALL PROBABILITY THE NATIVE ENZYME IS A HOMODIMER. IT ACTS OPTIMALLYAT PH 7.5 AND PHOSPHORYLATES HISTONES AND POLYSOMAL PROTEINS BUT NOT PROTAMINE, CASEIN OR ANY OF THE PROTEINS OF THE \"PH5\" FRACTION. AT HIGH (10- 5 M) ATP CONCENTRATIONS MG2+ IS THE MOST EFFICIENT ACTIVATING METAL WHILE AT LOW (10-9 M) ATP CONCENTRATIONS MN2+ IS. THE ACTIVITY OF THE PURIFIED KINASE IS AFFECTED BY THE PRESENCE OF ANY OF THE FOUR 3', 5' CYCLIC NUCLEOTIDES. THIS EFFECT WHICH MAY BE EITHER STIMULATORY OR INHIBITORY, DEPENDS ON THE CONCENTRATION OF ATP, ON THE TYPE OF ACTIVATING METAL EMPLOYED AS WELL AS ON THE SUBSTRATE USED. ON THE BASIS OF THE AFOREMENTIONED EFFECTS OF THE 3', 5' CYCLIC NUCLEOTIDES AND THE FACT THAT THE NATIVE ENZYME IS NOT DISSOCIATED INTO REGULATORY AND CATALYTIC SUBUNITS, THIS NOVEL KINASE NAMED CYCLIC NUCLEOTIDE- REGULATED PROTEIN KINASE (NRPK).","ΣΤΟ ΠΡΩΤΟ ΜΕΡΟΣ ΤΗΣ ΔΙΑΤΡΙΒΗΣ ΔΙΕΡΕΥΝΗΘΗΚΕ Η ΦΩΣΦΟΡΥΛΙΩΣΗ ΤΩΝ ΕΠΙΜΕΡΟΥΣ ΠΡΩΤΕΙΝΙΚΩΝ ΣΥΣΤΑΤΙΚΩΝ ΕΝΟΣ ΣΥΣΤΗΜΑΤΟΣ ΠΡΩΤΕΙΝΟΣΥΝΘΕΣΗΣ ΕΛΕΥΘΕΡΟΥ ΚΥΤΤΑΡΩΝ (ΠΟΛΥΣΩΜΑΤΑ, ΚΛΑΣΜΑ \"PH5\") ΑΠΟ ΣΥΚΩΤΙ ΠΟΝΤΙΚΟΥ ΚΑΘΩΣ ΚΑΙ Η ΕΠΙΔΡΑΣΗ ΔΙΑΦΟΡΩΝ ΠΑΡΑΓΟΝΤΩΝ ΠΟΥ ΤΗΝ ΕΠΗΡΕΑΖΟΥΝ. ΣΤΟ ΔΕΥΤΕΡΟ ΜΕΡΟΣ ΤΗΣ ΔΙΑΤΡΙΒΗΣ ΑΠΟΜΟΝΩΘΗΚΕ ΚΑΙ ΜΕΛΕΤΗΘΗΚΕ ΜΙΑ ΝΕΑ ΚΙΝΑΣΗ ΠΡΩΤΕΙΝΩΝ ΑΠΟ ΤΟ ΚΥΤΤΑΡΟΠΛΑΣΜΑ ΚΑΙ ΣΥΓΚΕΚΡΙΜΕΝΑ ΑΠΟ ΤΟ ΚΛΑΣΜΑ \"PH5\". Η ΚΙΝΑΣΗ ΑΥΤΗ ΤΩΝ ΠΡΩΤΕΙΝΩΝ ΕΙΝΑΙ ΚΙΝΑΣΗ ΣΕΡΙΝΗΣ- ΘΡΕΟΝΙΝΗΣ ΚΑΙ ΕΧΕΙ ΜΟΡΙΑΚΟΒΑΡΟΣ 90 KDA. ΠΕΡΙΕΧΕΙ ΜΙΑ ΑΥΤΟΦΩΣΦΟΡΥΛΙΟΥΜΕΝΗ ΥΠΟΜΟΝΑΔΑ ΤΩΝ 47 KDA ΚΑΙ ΓΙΑ ΤΟΛΟΓΟ ΑΥΤΟ ΚΑΤΑ ΠΑΣΑ ΠΙΘΑΝΟΤΗΤΑ ΤΟ ΔΡΑΣΤΙΚΟ ΕΝΖΥΜΟ ΕΙΝΑΙ ΕΝΑ ΟΜΟΔΙΜΕΡΕΣ. ΕΧΕΙ ΒΕΛΤΙΣΤΟ PH ΔΡΑΣΗΣ 7.5 ΚΑΙ ΦΩΣΦΟΡΥΛΙΩΝΕΙ ΙΣΤΟΝΕΣ ΚΑΙ ΡΙΒΟΣΗΜΙΚΕΣ ΠΡΩΤΕΙΝΕΣ ΑΛΛΑ ΟΧΙ ΚΑΖΕΙΝΗ, ΠΡΟΤΑΜΙΝΗ ΚΑΙ ΠΡΩΤΕΙΝΕΣ ΤΟΥ ΚΛΑΣΜΑΤΟΣ \"PH5\". ΣΕ ΨΗΛΕΣ ΣΥΓΚΕΝΤΡΩΣΕΙΣ ATP (10-5 Μ)ΔΡΑ ΚΑΛΥΤΕΡΑ ΠΑΡΟΥΣΙΑ MG2+, ΕΝΩ ΑΝΤΙΘΕΤΑ ΣΕ ΧΑΜΗΛΕΣ ΣΥΓΚΕΝΤΡΩΣΕΙΣATP (10-9 Μ) ΠΑΡΟΥΣΙΑ MN2+. Η ΔΡΑΣΗ ΤΗΣ ΚΙΝΑΣΗΣ ΕΠΗΡΕΑΖΕΤΑΙ ΑΠΟ ΤΗΝ ΠΑΡΟΥΣΙΑ ΤΩΝ 3', 5' ΚΥΚΛΙΚΩΝ ΝΟΥΚΛΕΟΤΙΔΙΩΝ ΚΑΙ ΤΟ ΑΠΟΤΕΛΕΣΜΑ ΕΞΑΡΤΑΤΑΙ ΤΟΣΟ ΑΠΟ ΤΗ ΣΥΓΚΕΝΤΡΩΣΗ ΤΟΥ ATP, ΟΣΟ ΚΑΙ ΑΠΟ ΤΟ ΜΕΤΑΛΛΟ ΠΟΥ ΧΡΗΣΙΜΟΠΟΙΕΙΤΑΙ ΩΣ ΕΝΕΡΓΟΠΟΙΗΤΗΣ ΚΑΘΩΣ ΚΑΙ ΑΠΟ ΤΗ ΦΥΣΗ ΤΟΥ ΥΠΟΣΤΡΩΜΑΤΟΣ. ΜΕ ΒΑΣΗ ΤΙΣ ΠΙΟ ΠΑΝΩ ΕΠΙΠΤΩΣΕΙΣ ΤΩΝ 3', 5' ΚΥΚΛΙΚΩΝ ΝΟΥΚΛΕΟΤΙΔΙΩΝ ΣΤΗ ΔΡΑΣΗ ΤΟΥ ΕΝΖΥΜΟΥ ΚΑΘΩΣ ΚΑΙ ΑΠΟ ΤΟ ΓΕΓΟΝΟΣ ΟΤΙ ΔΕΝ ΔΙΑΣΠΑΤΑΙ ΣΕ ΚΑΤΑΛΥΤΙΚΗ ΚΑΙ ΡΥΘΜΙΣΤΙΚΗ ΥΠΟΜΟΝΑΔΑ Η ΚΙΝΑΣΗ ΑΥΤΗ ΟΝΟΜΑΣΤΗΚΕ : ΚΙΝΑΣΗ ΠΟΥ Η ΔΡΑΣΗ ΤΗΣ ΡΥΘΜΙΖΕΤΑΙ ΑΠΟ ΚΥΚΛΙΚΑ ΝΟΥΚΛΕΟΤΙΔΙΑ (DNRPK, CYCLIC NUCLETIDE-REGULATED PROTEIN KINASE)."],"dc:identifier":["10.12681/eadd/1437","http://hdl.handle.net/10442/hedi/1437"],"dc:language":["gre"],"dc:publisher":["Aristotle University Of Thessaloniki (AUTH)","Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ)"],"dc:subject":["3', 5' CYCLIC NUCLEOTIDES","3', 5' ΚΥΚΛΙΚΑ ΝΟΥΚΛΕΟΤΙΔΙΑ","MOUSE LIVER","Protein kinases","Protein phosphorylation","Ribosomal proteins","ΚΙΝΑΣΗ ΠΡΩΤΕΙΝΩΝ","Ριβοσωμικές πρωτεΐνες","ΣΥΚΩΤΙ ΠΟΝΤΙΚΟΥ","Φωσφορυλίωση πρωτεινών","Φυσικές Επιστήμες","Χημεία","Natural Sciences","Chemical Sciences"],"dc:title":["ΦΩΣΦΟΡΥΛΙΩΣΗ ΠΡΩΤΕΙΝΩΝ ΣΕ ΣΥΣΤΗΜΑ ΠΡΩΤΕΙΝΟΣΥΝΘΕΣΗΣ ΕΛΕΥΘΕΡΟ ΚΥΤΤΑΡΩΝ ΑΠΟ ΣΥΚΩΤΙΠΟΝΤΙΚΟΥ. ΚΑΘΑΡΙΣΜΟΣ ΚΑΙ ΧΑΡΑΚΤΗΡΙΣΜΟΣ ΜΙΑΣ ΝΕΑΣ ΚΙΝΑΣΗΣ ΠΡΩΤΕΙΝΩΝ ΠΟΥ ΡΥΘΜΙΖΕΤΑΙ ΑΠΟ ΚΥΚΛΙΚΑ ΝΟΥΚΛΕΟΤΙΔΙΑ","PROTEIN PHOSPHORYLATION IN A CELL FREE SYSTEM OF PROTEIN SYNTHESIS FROM MOUSE LIVER. PURIFICATION AND CHARACTERIZATION OF A NOVEL PROTEIN KINASE REGULATED BY CYCLIC NUCLEOTIDES"],"dc:type":["PhD Thesis"]},"updated_at":"2026-07-24T02:24:56Z"}