Phosphorylation of adenosine 5'-monophosphate by a dialyzed cell-free extract from escherichia Coli

A cell-free extract of Escherichia coli, even after exhaustive dialysis, was capable of phosphorylating 5'-AMP to ADP and ATP. When cyclic AMP phosphodiesterase was present in the extract, the conversion of cyclic AMP to ADP and ATP occurred. If 3H or 32P-labeled 5'-AMP or cyclic AMP was added to the extract, a significant portion of the radioactivity was incorporated into the 3'-terminus of tRNA species. The phosphorylating capacity was sedimentable after centrifuging at 100,000 g for 3 hours. The pellet contained phosphate polymers which are neither DNA, RNA or proteins, while the supernate contained little of this material. The addition of authentic inorganic polyphosphates to the supernate restored the original phosphorylating capacity of the extract. Thus, it is concluded that the phosphorylating property is partly due to inorganic polyphosphates. A method for assaying total inorganic polyphosphates has been developed.

Name thesis:degree_name

Master of Science (M.Sc.)

Level thesis:degree_level

Master's

Discipline thesis:degree_discipline

Biology

Grantor dc:publisher

Carleton University

Year dc:date.issued

1978

Author dc:creator

• Chalykoff, Penu Peneff

Statement dc:rights

• Copyright © 1978 the author(s). Theses may be used for non-commercial research, educational, or related academic purposes only. Such uses include personal study, research, scholarship, and teaching. Theses may only be shared by linking to Carleton University Institutional Repository and no part may be used without proper attribution to the author. No part may be used for commercial purposes directly or indirectly via a for-profit platform; no adaptation or derivative works are permitted without consent from the copyright owner.

Language dc:language.iso

en

DOI

10.22215/etd/1978-12419

OAI identifier oai:identifier

oai:carleton.scholaris.ca:20.500.14718/27097