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Science 22 May 1981:
Vol. 212. no. 4497, pp. 939 - 941
DOI: 10.1126/science.7233189
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Articles

Science, Vol 212, Issue 4497, 939-941
Copyright © 1981 by American Association for the Advancement of Science

articles

Protozoan parasite of humans: surface membrane with externally disposed acid phosphatase

M Gottlieb and DM Dwyer

Plasma membranes isolated from the protozoan parasite Leishmania donovani were enriched in acid phosphatase (E.C. 3.1.3.2) activity. Cytochemically, the enzyme was distributed uniformly on the surface of intact cells and was localized on the external face of isolated membranes. Physical characteristics and orientation of the membrane-bound enzyme suggest that the organism is adapted for existence in hydrolytic environments.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Molecular Dissection of the Functional Domains of a Unique, Tartrate-resistant, Surface Membrane Acid Phosphatase in the Primitive Human Pathogen Leishmania donovani.
A. M. Shakarian, M. B. Joshi, E. Ghedin, and D. M. Dwyer (2002)
J. Biol. Chem. 277, 17994-18001
   Abstract »    Full Text »    PDF »
Enhanced metabolism of Leishmania donovani amastigotes at acid pH: an adaptation for intracellular growth.
A. Mukkada, J. Meade, T. Glaser, and P. Bonventre (1985)
Science 229, 1099-1101
   Abstract »    PDF »
Enzyme regulation in a trypanosomatid: effect of purine starvation on levels of 3'-nucleotidase activity.
M Gottlieb (1985)
Science 227, 72-74
   Abstract »    PDF »


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