The Partial Purification and Characterization of Adenosine Kinase from Entamoeba histolytica

Patricia A. Lobelle-RichDepartment of Biochemistry, Louisiana State University Medical Center, New Orleans, Louisiana 70112

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Richard E. ReevesDepartment of Biochemistry, Louisiana State University Medical Center, New Orleans, Louisiana 70112

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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.

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