Identification and partial characterization of an extracellular acid phosphatase activity of Leishmania donovani promastigotes.
An extracellular acid phosphatase was detected in the growth media of Leishmania donovani promastigotes. The enzyme was released at all stages of the growth cycle and in amounts which accounted for 90% of the total amount of this enzyme in the culture. The exoenzyme exhibited a pH optimum of 4.5 to 5.0 and was active with a variety of organic phosphates. The enzymatic activity was excluded from Sephacryl S-300 and was retained by ultrafilters with nominal molecular weight cutoffs of up to 300,000. The results of comparative studies indicated that the extracellular enzyme was distinct from a surface membrane-bound acid phosphatase of L. donovani promastigotes which has been previously described.
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D005110:Extracellular Space / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007891:Leishmania / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity
D000135:Acid Phosphatase