A nucleotidase from Leishmania tropica Promastigotes: partial purification and properties

Nucleotidase activity which had been found in various subcellular fractions of Leishmania tropica has been partially purified from the supernatant of the Triton X-100 treated pellet of the 100 000 g centrifugation of the L. tropica homogenate by CM-cellulose column chromatography, Con A-Sepharose affinity chromatography, isoelectrofocusing and column chromatography on Sephacryl S-300. The enzyme showed the characteristics of a nucleotidase (EC 3.1.3.31) with a broad substrate specificity. It was inhibited by the products of the reaction and by alpha, beta-methylene adenosine 5'diphosphate and adenosine 5'-9-thiomonophosphate. Nucleotidase activity of intact Leishmania cells and the inhibitory effect of Concanavalin A on the activity of the enzyme suggest also surface-associated properties of the enzyme.