ΑΠΟΜΟΝΩΣΗ ΚΑΙ ΧΑΡΑΚΤΗΡΙΣΜΟΣ ΤΗΣ ΚΙΝΑΣΗΣ ΚΑΖΕΙΝΗΣ ΙΙ ΑΠΟ ΣΠΛΗΝΑ ΠΑΙΔΙΩΝ ΜΕ ΜΕΣΟΓΕΙΑΚΗ ΑΝΑΙΜΙΑ

IN THE PRESENT STUDY CASEIN KINASE II WAS PURIFIED FROM CHILDREN'S SPLEEN, SUFFERING FROM BETA-THALASSEMIA MAJOR AND WAS CHARACTERIZED SDS POLYACRYLAMIDE GEL ELECTROPHORESIS AND ISOELECTRIC FOCUSING HAVE PROVED THAT THE ENZYME WAS HIGHLY PURIFIED. THE PURIFICATION STEPS INCLUDED ION EXCHANGE CHROMATOGRAPHY, AMMONIUM SULFATE FRACTIONATION AND MOLECULAR SIEVING. THE PURIFIED ENZYME PHOSPHORYLATES IN PREFERENCE ACIDIC PROTEINS, CASEIN, USING ATP AND GTP AS PHOSPHATEDONORS, IN THE PRESENCE OF MGCL2. THE ENZYME IS CAMP AND CGMP INDEPENDENT, HAS A MOLECULAR WEIGHT OF 43.000 AND PI 71. IT IS INHIBITED BY HEPARIN. BECAUSE OF THE ABOVE CHARACTERISTICS THIS ENZYME IS LISTED AMONG CASEIN KINASES II. THE PURIFIED ENZYME CAN BE USED AS A TOOL IN THE STUDY OF PHOSPHORYLATION, ONE OF THE MOST IMPORTANT POST- SYNTHETIC MODIFICATIONS OF THE CELL MACROMOLECULES.

Grantor dc:publisher

National and Kapodistrian University of Athens

Year dc:date

1986

Authors dc:creator

• Gounari, Antonia
• Γούναρη, Αντωνία

• Βιοχημεία
• ΚΙΝΑΣΗ ΚΑΖΕΙΝΗΣ
• Μεσογειακή αναιμία
• Σπλήνας
• Φωσφορυλίωση
• BETA THALASSEMIA MAJOR
• Casein kinase
• Phosphorylation
• Spleen
• Φυσικές Επιστήμες
• Βιολογία
• Natural Sciences
• Biological Sciences

Language dc:language

gre

Identifier

10.12681/eadd/0259

OAI identifier oai:identifier

oai:10442/0259