The Partial Purification and Characterization of Adenosine Kinase from Entamoeba histolytica *
- 1 September 1983
- journal article
- research article
- Published by American Society of Tropical Medicine and Hygiene in The American Journal of Tropical Medicine and Hygiene
- Vol. 32 (5) , 976-979
- https://doi.org/10.4269/ajtmh.1983.32.976
Abstract
Axenically grown Entamoeba histolytica was found to contain adenosine kinase. This organism lacks de novo purine biosynthetic pathways. Adenosine kinase provides the amoeba with a method for salvaging adenosine from ingested nucleosides or from degraded nucleotides. Adenosine kinase was purified 64-fold, by chromatography on Sephacryl S-200, DEAE-cellulose, and (C-8)-adenosine-agarose. The latter separated it from amebal adenylate kinase. Adenosine kinase has a molecular weight of 38,000 and requires glycerol for stability. It utilizes adenosine triphosphate to phosphorylate adenosine, and 7-deazaadenosine (tubercidin), but adenine 9-β-D-arabinofuranoside (ara-A) is not detectably phosphorylated. It requires Mg++ as a cofactor.This publication has 1 reference indexed in Scilit:
- Adenosine kinase from rabbit liver. I. Purification by affinity chromatography and propertiesJournal of Biological Chemistry, 1979