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Surface membrane localization of 3'- and 5'-nucleotidase activities in Leishmania donovani promastigotes.

Abstract：

:Distinct 3'- and 5'-nucleotidase activities were localized to the surface membrane of Leishmania donovani promastigotes using enzymatic reactions with live intact cells and fine structure enzyme-mediated cytochemical reactions with intact cells, cell homogenates, and isolated surface membranes. The results indicated that virtually all activity of both enzymes was restricted to the parasite surface membrane. Cytochemical localization results demonstrated that both activities were externally disposed on the intact organism, and were restricted to the external face of the isolated parasite surface membrane. The two activities were cytochemically differentiated by their substrate specificities and sensitivity to several inhibitors. On the basis of their cytochemical sensitivity to glutaraldehyde treatment, the two nucleotidase enzymes were distinguished from another external surface membrane enzyme, a nonspecific acid phosphatase. Results of the cytochemical assays further demonstrated the biochemical and structural asymmetry of the isolated parasite surface membrane with regard to the localization and distribution of the active sites of these two enzymes.

journal_name

Mol Biochem Parasitol

journal_title

Molecular and biochemical parasitology

authors

Dwyer DM,Gottlieb M

doi

10.1016/0166-6851(84)90002-1

subject

Has Abstract

pub_date

1984-02-01 00:00:00

pages

139-50

issue

2

eissn

0166-6851

issn

1872-9428

pii

0166-6851(84)90002-1

journal_volume

10

pub_type

杂志文章

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