{"id":{"repo_id":"greece","oai_identifier":"oai:10442/1112"},"canonical_url":"https://search.dev.ndltd.org/etd/greece/oai:10442/1112","repository":{"repo_id":"greece","name":"Greek National Archive of PhD Theses","base_url":"https://phdtheses.ekt.gr/eadd_oai/request"},"display":{"title":"ΦΩΣΦΑΤΑΣΗ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ ΚΑΙ ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗ ΣΤΟΝ ΑΝΘΡΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ","abstract":"FRUCTOSE 1,6-BISPHOSPHATASE (FRUCTOSE) HAS BEEN IDENTIFIED IN EXTRACTS OF HUMANTERM PLACENTA UNDER CONDITIONS WHERE THE PLACENTA WAS FROZEN IN LIQUID NITROGEN IMMEDIATELY AFTER DELIVERY . THE ENZYMATIC ACTIVITY 0.03 MMOLES FRU-P2/MIN/G TISSUE WAS FOUND TO HAVE AN ALKALINE PH OPTIMUM AND MW OF 26,000 DALTONS. THE MICHAELS-MENTEN CONSTANT FOR FRU-P2 WAS FOUND TO BE 2,6X10-5M AT PH 7,4 AMP, AS STRONG INHIBITOR OF FRU-P2ASES, INHIBITED THE ACTIVITY WITH A K1 3,3X10-4M AT PH 7,4. THESE RESULTS INDICATE THE PRESENCE OF A PROTELYSED FORM OF FRUCTOSE-1,6-BISPHOSPHATASE IN HUMAN TERM PLACENTA. ATP-DISPHOSPHOHYDROLASE (ATP-DPH) HAS BEEN ALSO IDENTIFIED IN HUMAN TERM PLACENTA ATP-DPH ACTIVITY WAS FOUND TO BE ASSOCIATED WITH A PARTICULATE FRACTION (P37). IT HYDROLYSES ATP TO AMI AND INORGANIC PHOSPHATE THROUGH ADP. THE PH OPTIMUM OF ATP-DPH IS 8,0-8,5. THE ENZYME IS ACTIVATED BY MG2+(IMM) BY NAF OR NAN3 WHILE INHIBITORS OF ATPASES, MYOKINASE ANDALKALINE PHOSPHATASE HAVE NO EFFECT. ATP-DPH DEGRADES ADP THUS PREVENTING PLATELET AGGREGATION AND BLOOD CLOTTING. THE PHYSIOLOGICAL ROLE OF THIS ENZYME WILLBE FURTHER INVESTIGATED WHEN THE ACTIVITY IS SOLUBILIZED AND PURIFIED.","abstract_html":"FRUCTOSE 1,6-BISPHOSPHATASE (FRUCTOSE) HAS BEEN IDENTIFIED IN EXTRACTS OF HUMANTERM PLACENTA UNDER CONDITIONS WHERE THE PLACENTA WAS FROZEN IN LIQUID NITROGEN IMMEDIATELY AFTER DELIVERY . THE ENZYMATIC ACTIVITY 0.03 MMOLES FRU-P2/MIN/G TISSUE WAS FOUND TO HAVE AN ALKALINE PH OPTIMUM AND MW OF 26,000 DALTONS. THE MICHAELS-MENTEN CONSTANT FOR FRU-P2 WAS FOUND TO BE 2,6X10-5M AT PH 7,4 AMP, AS STRONG INHIBITOR OF FRU-P2ASES, INHIBITED THE ACTIVITY WITH A K1 3,3X10-4M AT PH 7,4. THESE RESULTS INDICATE THE PRESENCE OF A PROTELYSED FORM OF FRUCTOSE-1,6-BISPHOSPHATASE IN HUMAN TERM PLACENTA. ATP-DISPHOSPHOHYDROLASE (ATP-DPH) HAS BEEN ALSO IDENTIFIED IN HUMAN TERM PLACENTA ATP-DPH ACTIVITY WAS FOUND TO BE ASSOCIATED WITH A PARTICULATE FRACTION (P37). IT HYDROLYSES ATP TO AMI AND INORGANIC PHOSPHATE THROUGH ADP. THE PH OPTIMUM OF ATP-DPH IS 8,0-8,5. THE ENZYME IS ACTIVATED BY MG2+(IMM) BY NAF OR NAN3 WHILE INHIBITORS OF ATPASES, MYOKINASE ANDALKALINE PHOSPHATASE HAVE NO EFFECT. ATP-DPH DEGRADES ADP THUS PREVENTING PLATELET AGGREGATION AND BLOOD CLOTTING. THE PHYSIOLOGICAL ROLE OF THIS ENZYME WILLBE FURTHER INVESTIGATED WHEN THE ACTIVITY IS SOLUBILIZED AND PURIFIED.","abstract_has_math":false,"creators":["Παπαμαρκάκη, Θωμαΐς"],"institution":"University of Ioannina","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1988,"date_issued":"1988","date_published":"1988","updated_at":"2026-07-24T02:24:43Z","subjects":["Ανθρώπινος πλακούντας","Απυράση","ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗ","ΦΩΣΦΑΤΑΣΗ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ","Apyrase","ATP diphosphohydrolase","FRUCTOSE-1,6-BISPHOSPHATASE","HUMAN TERM PLACENTA","Ιατρική και Επιστήμες Υγείας","Κλινική Ιατρική","Medical and Health Sciences","Clinical Medicine"],"languages":["gre"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["10.12681/eadd/1112"],"render_values":[{"text":"10.12681/eadd/1112","href":"https://doi.org/10.12681/eadd/1112","code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10442/hedi/1112","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Παπαμαρκάκη, Θωμαΐς"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["1988"]},{"key":"dc:publisher","label":"Institution","values":["University of Ioannina","Πανεπιστήμιο Ιωαννίνων"]},{"key":"dc:type","label":"Dc Type","values":["PhD Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Ανθρώπινος πλακούντας","Απυράση","ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗ","ΦΩΣΦΑΤΑΣΗ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ","Apyrase","ATP diphosphohydrolase","FRUCTOSE-1,6-BISPHOSPHATASE","HUMAN TERM PLACENTA","Ιατρική και Επιστήμες Υγείας","Κλινική Ιατρική","Medical and Health Sciences","Clinical Medicine"]}]},{"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/1112","http://hdl.handle.net/10442/hedi/1112"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["FRUCTOSE 1,6-BISPHOSPHATASE (FRUCTOSE) HAS BEEN IDENTIFIED IN EXTRACTS OF HUMANTERM PLACENTA UNDER CONDITIONS WHERE THE PLACENTA WAS FROZEN IN LIQUID NITROGEN IMMEDIATELY AFTER DELIVERY . THE ENZYMATIC ACTIVITY 0.03 MMOLES FRU-P2/MIN/G TISSUE WAS FOUND TO HAVE AN ALKALINE PH OPTIMUM AND MW OF 26,000 DALTONS. THE MICHAELS-MENTEN CONSTANT FOR FRU-P2 WAS FOUND TO BE 2,6X10-5M AT PH 7,4 AMP, AS STRONG INHIBITOR OF FRU-P2ASES, INHIBITED THE ACTIVITY WITH A K1 3,3X10-4M AT PH 7,4. THESE RESULTS INDICATE THE PRESENCE OF A PROTELYSED FORM OF FRUCTOSE-1,6-BISPHOSPHATASE IN HUMAN TERM PLACENTA. ATP-DISPHOSPHOHYDROLASE (ATP-DPH) HAS BEEN ALSO IDENTIFIED IN HUMAN TERM PLACENTA ATP-DPH ACTIVITY WAS FOUND TO BE ASSOCIATED WITH A PARTICULATE FRACTION (P37). IT HYDROLYSES ATP TO AMI AND INORGANIC PHOSPHATE THROUGH ADP. THE PH OPTIMUM OF ATP-DPH IS 8,0-8,5. THE ENZYME IS ACTIVATED BY MG2+(IMM) BY NAF OR NAN3 WHILE INHIBITORS OF ATPASES, MYOKINASE ANDALKALINE PHOSPHATASE HAVE NO EFFECT. ATP-DPH DEGRADES ADP THUS PREVENTING PLATELET AGGREGATION AND BLOOD CLOTTING. THE PHYSIOLOGICAL ROLE OF THIS ENZYME WILLBE FURTHER INVESTIGATED WHEN THE ACTIVITY IS SOLUBILIZED AND PURIFIED.","ΣΤΗΝ ΕΡΓΑΣΙΑ ΑΥΤΗ ΠΑΡΟΥΣΙΑΖΕΤΑΙ ΓΙΑ ΠΡΩΤΗ ΦΟΡΑ Η ΑΝΙΧΝΕΥΣΗ ΤΟΥ ΕΝΖΥΜΟΥ ΦΩΣΦΑΤΑΣΗ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ ΣΤΟΝ ΑΝΘΡΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ. Η ΕΝΕΡΓΟΤΗΤΑ ΠΟΥ ΠΡΟΣΔΙΟΡΙΣΤΗΚΕ ΕΧΕΙ ΤΑ ΠΑΡΑΚΑΤΩ ΧΑΡΑΚΤΗΡΙΣΤΙΚΑ: 0,03 U/G ΙΣΤΟΥ ΑΛΚΑΛΙΚΟ ΒΕΛΤΙΣΤΟ ΡΗ ΜΟΡΙΑΚΟ ΒΑΡΟΣ 26.000, ΚΜ=2,6Χ10-5Μ ΣΕ ΟΥΔΕΤΕΡΟ ΡΗ. ΒΡΕΘΗΚΕ ΕΠΙΣΗΣ ΟΤΙ ΤΟ ΕΝΖΥΜΟ ΣΤΟΝ ΠΛΑΚΟΥΝΤΑ ΑΝΑΣΤΕΛΛΕΤΑΙ ΑΠΟ ΤΟ ΑΜΡ ΜΕ ΚΙ=3,3Χ10-4 Μ ΣΕ ΡΗ=7,4 . ΕΠΙΣΗΣ ΑΝΑΣΤΕΛΛΕΤΑΙ ΑΠΟ ΠΕΡΙΣΣΕΙΑ ΤΟΥ ΥΠΟΣΤΡΩΜΑΤΟΣ ΤΗΣ 1,6- ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ. ΑΠΑΡΑΙΤΗΤΗ ΠΡΟΥΠΟΘΕΣΗ ΓΙΑ ΤΗΝ ΑΝΙΧΝΕΥΣΗ ΤΗΣ ΦΩΣΦΑΤΑΣΗΣ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ ΣΤΟΝ ΑΝΘΡΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ ΕΙΝΑΙ ΥΠΑΡΞΗ ΣΥΝΘΗΚΩΝ ΠΟΥ ΜΕΙΩΝΟΥΝ ΣΤΟ ΕΛΑΧΙΣΤΟΤΗ ΠΡΩΤΕΟΛΥΤΙΚΗ ΔΙΑΣΠΑΣΗ (ΥΓΡΟ ΑΖΩΤΟ). ΣΤΟΝ ΑΝΘΡΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ ΑΝΙΧΝΕΥΘΗΚΕ ΚΑΙ ΤΑΥΤΟΠΟΙΗΘΗΚΕ ΕΝΕΡΓΟΤΗΤΑ ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗΣ (DIP-DPH)F ΣΕ ΕΝΑ ΜΕΜΒΡΑΝΙΚΟ ΠΑΡΑΣΚΕΥΑΣΜΑ (Ρ37). Η ΕΝΕΡΓΟΤΗΤΑ ΑΥΤΗ ΥΔΡΟΛΥΕΙ ΤΟ ΑΤΡ ΣΕ ΑΜΡ ΚΑΙ ΑΝΟΡΓΑΝΟ ΦΩΣΦΟΡΙΚΟ (ΡΙ) ΜΕΣΩ ADP. Η ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗ ΕΝΕΡΓΟΠΟΙΕΙΤΑΙ ΑΠΟ MGH ΚΑΙ CA++ ΕΝΩ ΑΝΑΣΤΕΛΛΕΤΑΙ ΑΠΟ ΝΑΝ3 ΚΑΙ ΝΑΙ. ΑΝΑΣΤΟΛΕΙΣ ΑΤΡΑΣΩΝ, ΑΛΚΑΛΙΚΗΣ ΦΩΣΦΑΤΑΣΗΣ ΚΑΙ ΜΥΟΚΙΝΑΣΗΣ ΔΕΝ ΕΠΗΡΕΑΖΟΥΝ ΤΗΝ ΕΝΕΡΓΟΤΗΤΑ ΣΤΟΝ ΑΝΡΘΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ. Η ΑΤΡ-DPH ΕΧΕΙ ΜΕΓΑΛΗ ΦΥΣΙΟΛΟΓΙΚΗ ΣΗΜΑΣΙΑ ΔΙΟΤΙ ΥΔΡΟΛΥΕΙ ΤΟ ADP ΠΟΥ ΕΙΝΑΙ ΕΝΑΣ ΙΣΧΥΡΟΣ ΠΑΡΑΓΟΝΤΑΣΣΥΣΣΩΡΕΥΣΗΣ ΤΩΝ ΑΙΜΟΠΕΤΑΛΙΩΝ."]},{"key":"dc:title","label":"Title","values":["ΦΩΣΦΑΤΑΣΗ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ ΚΑΙ ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗ ΣΤΟΝ ΑΝΘΡΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ","FRUCTOSE 1,6-BISPHOSPHATASE AND ATP-DIPHOSPHOHYDROLASE IN HUMAN TERM PLACENTA"]}]}],"canonical_facts":{"dc:creator":["Παπαμαρκάκη, Θωμαΐς"],"dc:date":["1988"],"dc:description":["FRUCTOSE 1,6-BISPHOSPHATASE (FRUCTOSE) HAS BEEN IDENTIFIED IN EXTRACTS OF HUMANTERM PLACENTA UNDER CONDITIONS WHERE THE PLACENTA WAS FROZEN IN LIQUID NITROGEN IMMEDIATELY AFTER DELIVERY . THE ENZYMATIC ACTIVITY 0.03 MMOLES FRU-P2/MIN/G TISSUE WAS FOUND TO HAVE AN ALKALINE PH OPTIMUM AND MW OF 26,000 DALTONS. THE MICHAELS-MENTEN CONSTANT FOR FRU-P2 WAS FOUND TO BE 2,6X10-5M AT PH 7,4 AMP, AS STRONG INHIBITOR OF FRU-P2ASES, INHIBITED THE ACTIVITY WITH A K1 3,3X10-4M AT PH 7,4. THESE RESULTS INDICATE THE PRESENCE OF A PROTELYSED FORM OF FRUCTOSE-1,6-BISPHOSPHATASE IN HUMAN TERM PLACENTA. ATP-DISPHOSPHOHYDROLASE (ATP-DPH) HAS BEEN ALSO IDENTIFIED IN HUMAN TERM PLACENTA ATP-DPH ACTIVITY WAS FOUND TO BE ASSOCIATED WITH A PARTICULATE FRACTION (P37). IT HYDROLYSES ATP TO AMI AND INORGANIC PHOSPHATE THROUGH ADP. THE PH OPTIMUM OF ATP-DPH IS 8,0-8,5. THE ENZYME IS ACTIVATED BY MG2+(IMM) BY NAF OR NAN3 WHILE INHIBITORS OF ATPASES, MYOKINASE ANDALKALINE PHOSPHATASE HAVE NO EFFECT. ATP-DPH DEGRADES ADP THUS PREVENTING PLATELET AGGREGATION AND BLOOD CLOTTING. THE PHYSIOLOGICAL ROLE OF THIS ENZYME WILLBE FURTHER INVESTIGATED WHEN THE ACTIVITY IS SOLUBILIZED AND PURIFIED.","ΣΤΗΝ ΕΡΓΑΣΙΑ ΑΥΤΗ ΠΑΡΟΥΣΙΑΖΕΤΑΙ ΓΙΑ ΠΡΩΤΗ ΦΟΡΑ Η ΑΝΙΧΝΕΥΣΗ ΤΟΥ ΕΝΖΥΜΟΥ ΦΩΣΦΑΤΑΣΗ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ ΣΤΟΝ ΑΝΘΡΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ. Η ΕΝΕΡΓΟΤΗΤΑ ΠΟΥ ΠΡΟΣΔΙΟΡΙΣΤΗΚΕ ΕΧΕΙ ΤΑ ΠΑΡΑΚΑΤΩ ΧΑΡΑΚΤΗΡΙΣΤΙΚΑ: 0,03 U/G ΙΣΤΟΥ ΑΛΚΑΛΙΚΟ ΒΕΛΤΙΣΤΟ ΡΗ ΜΟΡΙΑΚΟ ΒΑΡΟΣ 26.000, ΚΜ=2,6Χ10-5Μ ΣΕ ΟΥΔΕΤΕΡΟ ΡΗ. ΒΡΕΘΗΚΕ ΕΠΙΣΗΣ ΟΤΙ ΤΟ ΕΝΖΥΜΟ ΣΤΟΝ ΠΛΑΚΟΥΝΤΑ ΑΝΑΣΤΕΛΛΕΤΑΙ ΑΠΟ ΤΟ ΑΜΡ ΜΕ ΚΙ=3,3Χ10-4 Μ ΣΕ ΡΗ=7,4 . ΕΠΙΣΗΣ ΑΝΑΣΤΕΛΛΕΤΑΙ ΑΠΟ ΠΕΡΙΣΣΕΙΑ ΤΟΥ ΥΠΟΣΤΡΩΜΑΤΟΣ ΤΗΣ 1,6- ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ. ΑΠΑΡΑΙΤΗΤΗ ΠΡΟΥΠΟΘΕΣΗ ΓΙΑ ΤΗΝ ΑΝΙΧΝΕΥΣΗ ΤΗΣ ΦΩΣΦΑΤΑΣΗΣ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ ΣΤΟΝ ΑΝΘΡΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ ΕΙΝΑΙ ΥΠΑΡΞΗ ΣΥΝΘΗΚΩΝ ΠΟΥ ΜΕΙΩΝΟΥΝ ΣΤΟ ΕΛΑΧΙΣΤΟΤΗ ΠΡΩΤΕΟΛΥΤΙΚΗ ΔΙΑΣΠΑΣΗ (ΥΓΡΟ ΑΖΩΤΟ). ΣΤΟΝ ΑΝΘΡΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ ΑΝΙΧΝΕΥΘΗΚΕ ΚΑΙ ΤΑΥΤΟΠΟΙΗΘΗΚΕ ΕΝΕΡΓΟΤΗΤΑ ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗΣ (DIP-DPH)F ΣΕ ΕΝΑ ΜΕΜΒΡΑΝΙΚΟ ΠΑΡΑΣΚΕΥΑΣΜΑ (Ρ37). Η ΕΝΕΡΓΟΤΗΤΑ ΑΥΤΗ ΥΔΡΟΛΥΕΙ ΤΟ ΑΤΡ ΣΕ ΑΜΡ ΚΑΙ ΑΝΟΡΓΑΝΟ ΦΩΣΦΟΡΙΚΟ (ΡΙ) ΜΕΣΩ ADP. Η ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗ ΕΝΕΡΓΟΠΟΙΕΙΤΑΙ ΑΠΟ MGH ΚΑΙ CA++ ΕΝΩ ΑΝΑΣΤΕΛΛΕΤΑΙ ΑΠΟ ΝΑΝ3 ΚΑΙ ΝΑΙ. ΑΝΑΣΤΟΛΕΙΣ ΑΤΡΑΣΩΝ, ΑΛΚΑΛΙΚΗΣ ΦΩΣΦΑΤΑΣΗΣ ΚΑΙ ΜΥΟΚΙΝΑΣΗΣ ΔΕΝ ΕΠΗΡΕΑΖΟΥΝ ΤΗΝ ΕΝΕΡΓΟΤΗΤΑ ΣΤΟΝ ΑΝΡΘΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ. Η ΑΤΡ-DPH ΕΧΕΙ ΜΕΓΑΛΗ ΦΥΣΙΟΛΟΓΙΚΗ ΣΗΜΑΣΙΑ ΔΙΟΤΙ ΥΔΡΟΛΥΕΙ ΤΟ ADP ΠΟΥ ΕΙΝΑΙ ΕΝΑΣ ΙΣΧΥΡΟΣ ΠΑΡΑΓΟΝΤΑΣΣΥΣΣΩΡΕΥΣΗΣ ΤΩΝ ΑΙΜΟΠΕΤΑΛΙΩΝ."],"dc:identifier":["10.12681/eadd/1112","http://hdl.handle.net/10442/hedi/1112"],"dc:language":["gre"],"dc:publisher":["University of Ioannina","Πανεπιστήμιο Ιωαννίνων"],"dc:subject":["Ανθρώπινος πλακούντας","Απυράση","ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗ","ΦΩΣΦΑΤΑΣΗ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ","Apyrase","ATP diphosphohydrolase","FRUCTOSE-1,6-BISPHOSPHATASE","HUMAN TERM PLACENTA","Ιατρική και Επιστήμες Υγείας","Κλινική Ιατρική","Medical and Health Sciences","Clinical Medicine"],"dc:title":["ΦΩΣΦΑΤΑΣΗ ΤΗΣ 1,6-ΔΙΦΩΣΦΟΡΙΚΗΣ ΦΡΟΥΚΤΟΖΗΣ ΚΑΙ ΑΤΡ-ΔΙΦΩΣΦΟΥΔΡΟΛΑΣΗ ΣΤΟΝ ΑΝΘΡΩΠΙΝΟ ΠΛΑΚΟΥΝΤΑ","FRUCTOSE 1,6-BISPHOSPHATASE AND ATP-DIPHOSPHOHYDROLASE IN HUMAN TERM PLACENTA"],"dc:type":["PhD Thesis"]},"updated_at":"2026-07-24T02:24:43Z"}