Comparison of extracellular acid phosphatases from various isolates of Leishmania.
Forty isolates of Leishmania, representing all major species infecting humans and one parasite of lizards, were examined for their ability to secrete an extracellular acid phosphatase activity. This enzyme, which was originally described and characterized from a Sudanese strain of L. donovani, was detected in the culture supernatants of all species of promastigotes examined except for L. major and L. tarentolae. There were quantitative differences among species in their levels of enzyme activity and in the sensitivity of the exoenzyme to inhibition by L(+) tartrate. Upon electrophoresis in nondenaturing polyacrylamide gels, extracellular acid phosphatase from L. braziliensis panamensis, L. tropica, and L. mexicana showed distinctive patterns which were similar for all isolates of a given species, while enzymes from L. donovani isolates differed from one another in relative electrophoretic mobility. Enzymes from all species appeared heterogeneous, showing either discrete multiple bands or single diffuse bands on gels stained for enzyme activity. Although the biological function of the extracellular acid phosphatase is presently unknown, the exoenzyme may be of value as a diagnostic or taxonomic characteristic.
D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007891:Leishmania / Q000201:enzymology*; D007893:Leishmania donovani / Q000201:enzymology; D007895:Leishmania tropica / Q000201:enzymology; D008116:Lizards / Q000469:parasitology; D013644:Tartrates / Q000494:pharmacology
D013644:Tartrates; D000135:Acid Phosphatase; C029768:tartaric acid