ΦΩΣΦΟΡΥΛΙΩΣΗ ΠΡΩΤΕΙΝΩΝ ΣΕ ΣΥΣΤΗΜΑ ΠΡΩΤΕΙΝΟΣΥΝΘΕΣΗΣ ΕΛΕΥΘΕΡΟ ΚΥΤΤΑΡΩΝ ΑΠΟ ΣΥΚΩΤΙΠΟΝΤΙΚΟΥ. ΚΑΘΑΡΙΣΜΟΣ ΚΑΙ ΧΑΡΑΚΤΗΡΙΣΜΟΣ ΜΙΑΣ ΝΕΑΣ ΚΙΝΑΣΗΣ ΠΡΩΤΕΙΝΩΝ ΠΟΥ ΡΥΘΜΙΖΕΤΑΙ ΑΠΟ ΚΥΚΛΙΚΑ ΝΟΥΚΛΕΟΤΙΔΙΑ

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).

Grantor dc:publisher

Aristotle University Of Thessaloniki (AUTH)

Year dc:date

1990

Authors dc:creator

• Nikolakaki, Eleni
• Νικολακάκη, Ελένη

• 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

Language dc:language

gre

Identifier

10.12681/eadd/1437

OAI identifier oai:identifier

oai:10442/1437