{"id":{"repo_id":"greece","oai_identifier":"oai:10442/0729"},"canonical_url":"https://search.dev.ndltd.org/etd/greece/oai:10442/0729","repository":{"repo_id":"greece","name":"Greek National Archive of PhD Theses","base_url":"https://phdtheses.ekt.gr/eadd_oai/request"},"display":{"title":"ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΑΠΟ ΛΕΙΟ ΜΥΙΚΟ ΙΣΤΟ ΣΤΟΜΑΧΙΟΥ ΚΟΤΑΣ: ΑΠΟΜΟΝΩΣΗ ΚΑΙ ΜΕΛΕΤΗ ΤΩΝ ΚΑΤΑΛΥΤΙΚΩΝ ΚΑΙ ΔΟΜΙΚΩΝ ΙΔΙΟΤΗΤΩΝ ΤΗΣ","abstract":"THE SCOPE OF THIS WORK IS TO FACILITATE THE UNDERSTANDING OF ENZYMATIC REGULATION OF GLYCOGEN BREAKDOWN IN SMOOTH MUSCLE CELLS . PHOSPORYLASE KINASE FROM CHICKEN GIZZARD WAS PURIFIED BY A PROCEDURE INVOLVING AMMONIUM SULFATE FRACTIONATION 5'-AMP SEPHAROSE 4B AFFINITY CHROMATOGRAPHY COLUMN AND ULTRACENTRIFUGATION INGLYCEROL GRADIENT DENSITY CHICKEN GIZZARD PHOSPHORYLASE KINASE PRESENTS DIFFERENT STRUCTURAL AND CATALYTIC PROPERTIES IN DELATION TO THOSE FOUND FOR THE RABBIT SKELETAL MUSCLE ISOENZYME. ALTHOUGH BOTH KINASES HAVE THE SAME HIGH MOLECULAR WEIGHT (1.3 X 106), THE SUBUNIT STRUCTURE OF THESE ISOENZYMES ARE DIFFERENT. ELECTROPHORETIC DATA INDICATES THAT CHICHEN GIZZARD PHOSPHORYLASE KINASE DOES NOT COMPRISE Γ SUBUNIT IN ITS STRUCTURE WHICH IS THE CATALYTIC SUBUNIT OF RABBITSKELETAL MUSCLE ISOENZYME. GIZZARD PHOSPHORYLASE KINASE SHOWED AN EXTREMELY HIGH AFFINITY FOR ITS PROTEIN SUBSTRATE PHOSPHORYLASE B . THIS ENZYME DOES NOT EXIST IN A PHOSPHORYLATED OR ACTIVATED FORM, WHILE IS AFFECTED BY CA2+. THESE DATA SUGGEST THAT THE ACTIVATION OF CHICKEN GIZZARD PHOSPHRYLASE KINASE IS REGULATED BY A MECHANISM INVOLVING THE CA2+ SYSTEM RATHER, THAN THE PHOSPHORYLATION SYSTEM.","abstract_html":"THE SCOPE OF THIS WORK IS TO FACILITATE THE UNDERSTANDING OF ENZYMATIC REGULATION OF GLYCOGEN BREAKDOWN IN SMOOTH MUSCLE CELLS . PHOSPORYLASE KINASE FROM CHICKEN GIZZARD WAS PURIFIED BY A PROCEDURE INVOLVING AMMONIUM SULFATE FRACTIONATION 5'-AMP SEPHAROSE 4B AFFINITY CHROMATOGRAPHY COLUMN AND ULTRACENTRIFUGATION INGLYCEROL GRADIENT DENSITY CHICKEN GIZZARD PHOSPHORYLASE KINASE PRESENTS DIFFERENT STRUCTURAL AND CATALYTIC PROPERTIES IN DELATION TO THOSE FOUND FOR THE RABBIT SKELETAL MUSCLE ISOENZYME. ALTHOUGH BOTH KINASES HAVE THE SAME HIGH MOLECULAR WEIGHT (1.3 X 106), THE SUBUNIT STRUCTURE OF THESE ISOENZYMES ARE DIFFERENT. ELECTROPHORETIC DATA INDICATES THAT CHICHEN GIZZARD PHOSPHORYLASE KINASE DOES NOT COMPRISE Γ SUBUNIT IN ITS STRUCTURE WHICH IS THE CATALYTIC SUBUNIT OF RABBITSKELETAL MUSCLE ISOENZYME. GIZZARD PHOSPHORYLASE KINASE SHOWED AN EXTREMELY HIGH AFFINITY FOR ITS PROTEIN SUBSTRATE PHOSPHORYLASE B . THIS ENZYME DOES NOT EXIST IN A PHOSPHORYLATED OR ACTIVATED FORM, WHILE IS AFFECTED BY CA2+. THESE DATA SUGGEST THAT THE ACTIVATION OF CHICKEN GIZZARD PHOSPHRYLASE KINASE IS REGULATED BY A MECHANISM INVOLVING THE CA2+ SYSTEM RATHER, THAN THE PHOSPHORYLATION SYSTEM.","abstract_has_math":false,"creators":["Nikolaropoulos, Stathis","Νικολαρόπουλος, Στάθης"],"institution":"National and Kapodistrian University of Athens","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":"2026-07-24T02:25:27Z","subjects":["Κινάση της φωσφορυλάσης","ΛΕΙΟΙ ΜΥΕΣ","Μεταβολισμός γλυκογόνου","Glycogen metabolism","Phosphorylase kinase","SMOOTH MUSCLE","Φυσικές Επιστήμες","Βιολογία","Natural Sciences","Biological Sciences"],"languages":["gre"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["10.12681/eadd/0729"],"render_values":[{"text":"10.12681/eadd/0729","href":"https://doi.org/10.12681/eadd/0729","code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10442/hedi/0729","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Nikolaropoulos, Stathis","Νικολαρόπουλος, Στάθης"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["1988"]},{"key":"dc:publisher","label":"Institution","values":["National and Kapodistrian University of Athens","Εθνικό και Καποδιστριακό Πανεπιστήμιο Αθηνών (ΕΚΠΑ)"]},{"key":"dc:type","label":"Dc Type","values":["PhD Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Κινάση της φωσφορυλάσης","ΛΕΙΟΙ ΜΥΕΣ","Μεταβολισμός γλυκογόνου","Glycogen metabolism","Phosphorylase kinase","SMOOTH MUSCLE","Φυσικές Επιστήμες","Βιολογία","Natural Sciences","Biological 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/0729","http://hdl.handle.net/10442/hedi/0729"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["THE SCOPE OF THIS WORK IS TO FACILITATE THE UNDERSTANDING OF ENZYMATIC REGULATION OF GLYCOGEN BREAKDOWN IN SMOOTH MUSCLE CELLS . PHOSPORYLASE KINASE FROM CHICKEN GIZZARD WAS PURIFIED BY A PROCEDURE INVOLVING AMMONIUM SULFATE FRACTIONATION 5'-AMP SEPHAROSE 4B AFFINITY CHROMATOGRAPHY COLUMN AND ULTRACENTRIFUGATION INGLYCEROL GRADIENT DENSITY CHICKEN GIZZARD PHOSPHORYLASE KINASE PRESENTS DIFFERENT STRUCTURAL AND CATALYTIC PROPERTIES IN DELATION TO THOSE FOUND FOR THE RABBIT SKELETAL MUSCLE ISOENZYME. ALTHOUGH BOTH KINASES HAVE THE SAME HIGH MOLECULAR WEIGHT (1.3 X 106), THE SUBUNIT STRUCTURE OF THESE ISOENZYMES ARE DIFFERENT. ELECTROPHORETIC DATA INDICATES THAT CHICHEN GIZZARD PHOSPHORYLASE KINASE DOES NOT COMPRISE Γ SUBUNIT IN ITS STRUCTURE WHICH IS THE CATALYTIC SUBUNIT OF RABBITSKELETAL MUSCLE ISOENZYME. GIZZARD PHOSPHORYLASE KINASE SHOWED AN EXTREMELY HIGH AFFINITY FOR ITS PROTEIN SUBSTRATE PHOSPHORYLASE B . THIS ENZYME DOES NOT EXIST IN A PHOSPHORYLATED OR ACTIVATED FORM, WHILE IS AFFECTED BY CA2+. THESE DATA SUGGEST THAT THE ACTIVATION OF CHICKEN GIZZARD PHOSPHRYLASE KINASE IS REGULATED BY A MECHANISM INVOLVING THE CA2+ SYSTEM RATHER, THAN THE PHOSPHORYLATION SYSTEM.","Η ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ (ΣΤΟΜΑΧΙ ΚΟΤΑΣ) ΔΕΝ ΕΧΕΙ ΑΠΟΜΟΝΩΘΕΙ ΚΑΙ ΜΕΛΕΤΗΘΕΙ. ΤΟ ΕΝΖΥΜΟ ΑΠΟΜΟΝΩΝΕΤΑΙ ΜΕ ΚΑΘΙΖΗΣΗ ΜΕ ΘΕΙΙΚΟ ΑΜΜΩΝΙΟ, 5' ΑΜΡ SEPHAROSE 4B ΧΡΩΜΑΤΟΓΡΑΦΙΑ ΚΑΙ ΥΠΕΡΦΥΓΟΚΕΝΤΡΗΣΗ ΣΕ ΒΑΘΜΙΔΩΣΗ ΠΥΚΝΟΤΗΤΑΣ ΓΛΥΚΕΡΟΛΗΣ. Η ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ ΕΜΦΑΝΙΖΕΙ ΑΞΙΟΣΗΜΕΙΩΤΑ ΔΙΑΦΟΡΕΤΙΚΕΣ ΔΟΜΙΚΕΣ ΚΑΙ ΚΑΤΑΛΥΤΙΚΕΣ ΙΔΙΟΤΗΤΕΣ ΣΕ ΣΧΕΣΗ ΜΕ ΤΟ ΙΣΟΕΝΖΥΜΟ ΤΩΝ ΣΚΕΛΕΤΙΚΩΝ ΜΥΩΝ ΚΟΥΝΕΛΙΟΥ. ΑΝ ΚΑΙ ΟΙ ΔΥΟ ΚΙΝΑΣΕΣ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΕΧΟΥΝ ΠΑΡΟΜΟΙΟ ΜΟΡΙΑΚΟ ΒΑΡΟΣ (1.3 Χ 106). Η ΔΟΜΗ ΤΩΝ ΥΠΟΜΟΝΑΔΩΝ ΤΟΥΣ ΕΙΝΑΙ ΔΙΑΦΟΡΕΤΙΚΗ. ΗΛΕΚΤΡΟΦΟΡΗΤΙΚΑ ΔΕΔΟΜΕΝΑ ΥΠΟΔΕΙΚΝΥΟΥ ΟΤΙ Η ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ ΔΕΝ ΣΥΜΠΕΡΙΛΑΜΒΑΝΕΙΣΤΗ ΔΟΜΗ ΤΗΣ ΤΗΝ Γ ΥΠΟΜΟΝΑΔΑ ΠΟΥ ΕΙΝΑΙ Η ΚΑΤΑΛΥΤΙΚΗ ΥΠΟΜΟΝΑΔΑ ΤΟΥ ΙΣΟΕΝΖΥΜΟΥ ΤΩΝ ΣΚΕΛΕΤΙΚΩΝ ΜΥΩΝ. ΕΠΙΠΛΕΟΝ Η ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ ΕΜΦΑΝΙΖΕΙΕΞΑΙΡΕΤΙΚΑ ΜΕΓΑΛΗ ΣΥΓΓΕΝΕΙΑ ΓΙΑ ΤΟ ΥΠΟΣΤΡΩΜΑ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ Β. ΤΟ ΕΝΖΥΜΟ ΔΕΝΥΠΑΡΧΕΙ ΣΕ ΜΙΑ ΦΩΣΦΟΡΥΛΙΩΜΕΝΗ 'Η ΕΝΕΡΓΟΠΟΙΗΜΕΝΗ ΜΟΡΦΗ, ΕΝΩ ΕΠΗΡΕΑΖΕΤΑΙ ΑΠΟ ΤΗΝΥΠΑΡΞΗ ΙΟΝΤΩΝ CA2+. ΤΑ ΔΕΔΟΜΕΝΑ ΑΥΤΑ ΥΠΟΔΕΙΚΝΥΟΥΝ ΟΤΙ Η ΕΝΕΡΓΟΠΟΙΗΣΗ ΤΗΣ ΚΙΝΑΣΗΣ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ ΓΙΝΕΤΑΙ ΜΑΛΛΟΝ ΔΙΑ ΜΕΣΟΥ ΤΩΝ ΙΟΝΤΩΝ CA2+, ΠΑΡΑ ΜΕΣΩ ΜΗΧΑΝΙΣΜΟΥ ΦΩΣΦΟΡΥΛΙΩΣΗΣ."]},{"key":"dc:title","label":"Title","values":["ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΑΠΟ ΛΕΙΟ ΜΥΙΚΟ ΙΣΤΟ ΣΤΟΜΑΧΙΟΥ ΚΟΤΑΣ: ΑΠΟΜΟΝΩΣΗ ΚΑΙ ΜΕΛΕΤΗ ΤΩΝ ΚΑΤΑΛΥΤΙΚΩΝ ΚΑΙ ΔΟΜΙΚΩΝ ΙΔΙΟΤΗΤΩΝ ΤΗΣ","PHOSPHORYLASE KINASE FROM SMOOTH MUSCLE (CHICKEN GIZZARD) PURIFICATION AND CHARACTERIZATION OF STRUCTURAL AND CATALYTICAL PROPERTIES"]}]}],"canonical_facts":{"dc:creator":["Nikolaropoulos, Stathis","Νικολαρόπουλος, Στάθης"],"dc:date":["1988"],"dc:description":["THE SCOPE OF THIS WORK IS TO FACILITATE THE UNDERSTANDING OF ENZYMATIC REGULATION OF GLYCOGEN BREAKDOWN IN SMOOTH MUSCLE CELLS . PHOSPORYLASE KINASE FROM CHICKEN GIZZARD WAS PURIFIED BY A PROCEDURE INVOLVING AMMONIUM SULFATE FRACTIONATION 5'-AMP SEPHAROSE 4B AFFINITY CHROMATOGRAPHY COLUMN AND ULTRACENTRIFUGATION INGLYCEROL GRADIENT DENSITY CHICKEN GIZZARD PHOSPHORYLASE KINASE PRESENTS DIFFERENT STRUCTURAL AND CATALYTIC PROPERTIES IN DELATION TO THOSE FOUND FOR THE RABBIT SKELETAL MUSCLE ISOENZYME. ALTHOUGH BOTH KINASES HAVE THE SAME HIGH MOLECULAR WEIGHT (1.3 X 106), THE SUBUNIT STRUCTURE OF THESE ISOENZYMES ARE DIFFERENT. ELECTROPHORETIC DATA INDICATES THAT CHICHEN GIZZARD PHOSPHORYLASE KINASE DOES NOT COMPRISE Γ SUBUNIT IN ITS STRUCTURE WHICH IS THE CATALYTIC SUBUNIT OF RABBITSKELETAL MUSCLE ISOENZYME. GIZZARD PHOSPHORYLASE KINASE SHOWED AN EXTREMELY HIGH AFFINITY FOR ITS PROTEIN SUBSTRATE PHOSPHORYLASE B . THIS ENZYME DOES NOT EXIST IN A PHOSPHORYLATED OR ACTIVATED FORM, WHILE IS AFFECTED BY CA2+. THESE DATA SUGGEST THAT THE ACTIVATION OF CHICKEN GIZZARD PHOSPHRYLASE KINASE IS REGULATED BY A MECHANISM INVOLVING THE CA2+ SYSTEM RATHER, THAN THE PHOSPHORYLATION SYSTEM.","Η ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ (ΣΤΟΜΑΧΙ ΚΟΤΑΣ) ΔΕΝ ΕΧΕΙ ΑΠΟΜΟΝΩΘΕΙ ΚΑΙ ΜΕΛΕΤΗΘΕΙ. ΤΟ ΕΝΖΥΜΟ ΑΠΟΜΟΝΩΝΕΤΑΙ ΜΕ ΚΑΘΙΖΗΣΗ ΜΕ ΘΕΙΙΚΟ ΑΜΜΩΝΙΟ, 5' ΑΜΡ SEPHAROSE 4B ΧΡΩΜΑΤΟΓΡΑΦΙΑ ΚΑΙ ΥΠΕΡΦΥΓΟΚΕΝΤΡΗΣΗ ΣΕ ΒΑΘΜΙΔΩΣΗ ΠΥΚΝΟΤΗΤΑΣ ΓΛΥΚΕΡΟΛΗΣ. Η ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ ΕΜΦΑΝΙΖΕΙ ΑΞΙΟΣΗΜΕΙΩΤΑ ΔΙΑΦΟΡΕΤΙΚΕΣ ΔΟΜΙΚΕΣ ΚΑΙ ΚΑΤΑΛΥΤΙΚΕΣ ΙΔΙΟΤΗΤΕΣ ΣΕ ΣΧΕΣΗ ΜΕ ΤΟ ΙΣΟΕΝΖΥΜΟ ΤΩΝ ΣΚΕΛΕΤΙΚΩΝ ΜΥΩΝ ΚΟΥΝΕΛΙΟΥ. ΑΝ ΚΑΙ ΟΙ ΔΥΟ ΚΙΝΑΣΕΣ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΕΧΟΥΝ ΠΑΡΟΜΟΙΟ ΜΟΡΙΑΚΟ ΒΑΡΟΣ (1.3 Χ 106). Η ΔΟΜΗ ΤΩΝ ΥΠΟΜΟΝΑΔΩΝ ΤΟΥΣ ΕΙΝΑΙ ΔΙΑΦΟΡΕΤΙΚΗ. ΗΛΕΚΤΡΟΦΟΡΗΤΙΚΑ ΔΕΔΟΜΕΝΑ ΥΠΟΔΕΙΚΝΥΟΥ ΟΤΙ Η ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ ΔΕΝ ΣΥΜΠΕΡΙΛΑΜΒΑΝΕΙΣΤΗ ΔΟΜΗ ΤΗΣ ΤΗΝ Γ ΥΠΟΜΟΝΑΔΑ ΠΟΥ ΕΙΝΑΙ Η ΚΑΤΑΛΥΤΙΚΗ ΥΠΟΜΟΝΑΔΑ ΤΟΥ ΙΣΟΕΝΖΥΜΟΥ ΤΩΝ ΣΚΕΛΕΤΙΚΩΝ ΜΥΩΝ. ΕΠΙΠΛΕΟΝ Η ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ ΕΜΦΑΝΙΖΕΙΕΞΑΙΡΕΤΙΚΑ ΜΕΓΑΛΗ ΣΥΓΓΕΝΕΙΑ ΓΙΑ ΤΟ ΥΠΟΣΤΡΩΜΑ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ Β. ΤΟ ΕΝΖΥΜΟ ΔΕΝΥΠΑΡΧΕΙ ΣΕ ΜΙΑ ΦΩΣΦΟΡΥΛΙΩΜΕΝΗ 'Η ΕΝΕΡΓΟΠΟΙΗΜΕΝΗ ΜΟΡΦΗ, ΕΝΩ ΕΠΗΡΕΑΖΕΤΑΙ ΑΠΟ ΤΗΝΥΠΑΡΞΗ ΙΟΝΤΩΝ CA2+. ΤΑ ΔΕΔΟΜΕΝΑ ΑΥΤΑ ΥΠΟΔΕΙΚΝΥΟΥΝ ΟΤΙ Η ΕΝΕΡΓΟΠΟΙΗΣΗ ΤΗΣ ΚΙΝΑΣΗΣ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΤΩΝ ΛΕΙΩΝ ΜΥΩΝ ΓΙΝΕΤΑΙ ΜΑΛΛΟΝ ΔΙΑ ΜΕΣΟΥ ΤΩΝ ΙΟΝΤΩΝ CA2+, ΠΑΡΑ ΜΕΣΩ ΜΗΧΑΝΙΣΜΟΥ ΦΩΣΦΟΡΥΛΙΩΣΗΣ."],"dc:identifier":["10.12681/eadd/0729","http://hdl.handle.net/10442/hedi/0729"],"dc:language":["gre"],"dc:publisher":["National and Kapodistrian University of Athens","Εθνικό και Καποδιστριακό Πανεπιστήμιο Αθηνών (ΕΚΠΑ)"],"dc:subject":["Κινάση της φωσφορυλάσης","ΛΕΙΟΙ ΜΥΕΣ","Μεταβολισμός γλυκογόνου","Glycogen metabolism","Phosphorylase kinase","SMOOTH MUSCLE","Φυσικές Επιστήμες","Βιολογία","Natural Sciences","Biological Sciences"],"dc:title":["ΚΙΝΑΣΗ ΤΗΣ ΦΩΣΦΟΡΥΛΑΣΗΣ ΑΠΟ ΛΕΙΟ ΜΥΙΚΟ ΙΣΤΟ ΣΤΟΜΑΧΙΟΥ ΚΟΤΑΣ: ΑΠΟΜΟΝΩΣΗ ΚΑΙ ΜΕΛΕΤΗ ΤΩΝ ΚΑΤΑΛΥΤΙΚΩΝ ΚΑΙ ΔΟΜΙΚΩΝ ΙΔΙΟΤΗΤΩΝ ΤΗΣ","PHOSPHORYLASE KINASE FROM SMOOTH MUSCLE (CHICKEN GIZZARD) PURIFICATION AND CHARACTERIZATION OF STRUCTURAL AND CATALYTICAL PROPERTIES"],"dc:type":["PhD Thesis"]},"updated_at":"2026-07-24T02:25:27Z"}