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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.
N M Pereira, and
E Königk
May 1987,
Molecular and biochemical parasitology,
N M Pereira, and
E Königk
July 1991,
Molecular and biochemical parasitology,
N M Pereira, and
E Königk
July 1995,
Molecular and cellular biochemistry,
N M Pereira, and
E Königk
June 1990,
Journal of general microbiology,
N M Pereira, and
E Königk
February 1976,
Experimental parasitology,
N M Pereira, and
E Königk
June 1977,
Experimental parasitology,
N M Pereira, and
E Königk
February 1979,
The Journal of protozoology,
N M Pereira, and
E Königk
January 1983,
Molecular and biochemical parasitology,
N M Pereira, and
E Königk
October 1974,
The Journal of protozoology,
N M Pereira, and
E Königk
March 1979,
Tropenmedizin und Parasitologie,
