Phosphomonoesterases of Leishmania mexicana mexicana and other flagellates.

Amastigotes and log-phase promastigotes of Leishmania mexicana mexicana contained distinct acid phosphatase, 3'-nucleotidase and 5'-nucleotidase activities, distinguishable by their response to pH and inhibitors. Both tartrate-sensitive and tartrate-resistant acid phosphatase were present in the two forms, amastigotes possessed less tartrate-resistant acid phosphatase than promastigotes. A tartrate-sensitive acid phosphatase was secreted into the medium in large amounts during the growth in vitro of L. m. mexicana promastigotes. The 5'-nucleotidase activity of both parasite forms was inhibited by ammonium molybdate, sodium tartrate and, to less extent, by sodium fluoride whereas 3'-nucleotidase was inhibited by EDTA. All three activities were shown to be present on the external surface of both amastigotes and promastigotes. The three phosphomonoesterase activities were also detected in extracts of L. m. amazonensis, L. donovani, L. tarentolae, Crithidia fasciculata, Herpetomonas muscarum muscarum, H.m. ingenoplastis and Trichomitus batrachorum whereas 5'-nucleotidase was not detected in Trypanosoma brucei brucei extract and 3'-nucleotidase was absent from extracts of Trichomonas vaginalis and Tritrichomonas foetus.