PMID: 3762593Sep 1, 1986Paper

Purification and characterization of the extracellular acid phosphatase of Leishmania donovani

Molecular and Biochemical Parasitology
J K LovelaceM Gottlieb

Abstract

A tartrate sensitive acid phosphatase activity was purified from culture supernatants of Leishmania donovani promastigotes grown in a macromolecule-free defined medium. Purification was accomplished by ultrafiltration, lentil lectin affinity chromatography, and sucrose density gradient ultracentrifugation. This enzyme was determined to be an acid glycoprotein containing 0.37 mg hexose per mg protein. A molecular weight of 134 000 by sucrose density gradient centrifugation was observed, although on molecular sieve chromatography the enzyme eluted with an apparent molecular weight of greater than 700 000. The specific activity of the purified enzyme was greater than 200 mumol min-1(mg protein)-1 when assayed with 4-methylumbelliferylphosphate as the substrate. In addition to various hexose phosphates, the enzyme hydrolyzed phosphorylated amino acids, in particular phosphotyrosine. The purified enzyme was heterodisperse with respect to both protein and activity staining patterns upon polyacrylamide gel electrophoresis.

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Citations

Apr 21, 2010·Parasitology Research·Alma R Escalona-MontañoMaria M Aguirre-García
May 1, 1993·Acta Tropica·S F Moody
Jan 2, 1987·Molecular and Biochemical Parasitology·J K Lovelace, M Gottlieb
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Dec 1, 1988·Microbiological Reviews·R H GlewA T Remaley

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