Abstract
3′-nucleotidase (3′N”Q is an externally oriented surface membrane enzyme of Leishmania donovani.1,2 The enzyme is a glycoprotein of apparent Mr=43,000, capable of hydrolyzing 3′-nucleotides and also exhibits exonuclease activity.1–3 As Leishmania have an absolute requirement for preformed purines, it has been suggested that the 3′NT might function in the acquisition of these essential nutrients from the growth medium.1,2 It was recently shown, in a related trypanosomatid, Crithidia fasciculate, that 3′NT activity was regulated by the levels of exogenously supplied purines.4 Similar regulation of 3′NT activity was observed with L. donovani in the current study. To facilitate the further characterization of this enzyme, a rabbit antiserum was rasied against the 3′NT isolated from L. donovani promastigotes. Results of immunochemical studies with this antiserum are presented in this report.
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References
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© 1989 Springer Science+Business Media New York
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Pastakia, K.B., Dwyer, D.M. (1989). Immunochemical Characterization of the Leishmania Donovani 3′-Nucleotidase. In: Hart, D.T. (eds) Leishmaniasis. NATO ASI Series, vol 171. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1575-9_80
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DOI: https://doi.org/10.1007/978-1-4613-1575-9_80
Publisher Name: Springer, Boston, MA
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