PURIFICATION AND PROPERTIES OF ADENOSINE NUCLEOSIDASES FROM TEA LEAVES

Three adenosine nucleosidases (adenosine ribohydrolase, EC 3.2.2.7) with high substrate specificity were isolated from the extracts of tea leaves by a procedure including fractionation with ammonium sulfate, column chromatography on DEAE- and CM-cellulose, and gel filtration on Sephadex G-100. They were designated adenosine nucleosidase I, II and III, respectively, and their properties were characterized. Among the naturally occurring nucleosides only adenosine and 2'-deoxyadenosine were hydrolyzed by these three enzymes and cleavage rate of the N-glycosidic bond in 2'-deoxyadenosine was three or four times greater than that in adenosine. © 1979 Taylor & Francis Group, LLC.