1983
DOI: 10.4269/ajtmh.1983.32.976
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The Partial Purification and Characterization of Adenosine Kinase from Entamoeba histolytica *

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 … Show more

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Cited by 14 publications
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“…These workers also suggested the presence of two nucleoside phosphorylases, one active on adenosine and the other on inosine, distinguishable by their different responses to pH and their sensitivity to inhibitors. Adenosine kinase has been purified from E. histolytica [156] and shown to have activity towards the adenosine analogue tubercidin, but not arabinosyladenine. Both compounds inhibit the growth of E. histolytica [157], although the mechanism by which these compounds exert their effect remains to be determined.…”
Section: Entamoeba Histolyticamentioning
confidence: 99%
“…These workers also suggested the presence of two nucleoside phosphorylases, one active on adenosine and the other on inosine, distinguishable by their different responses to pH and their sensitivity to inhibitors. Adenosine kinase has been purified from E. histolytica [156] and shown to have activity towards the adenosine analogue tubercidin, but not arabinosyladenine. Both compounds inhibit the growth of E. histolytica [157], although the mechanism by which these compounds exert their effect remains to be determined.…”
Section: Entamoeba Histolyticamentioning
confidence: 99%