Open AccessA major cysteine proteinase is developmentally regulated in Trypanosoma cruzi
Author(s) -
Campetella Oscar,
Martínez Javier,
Cazzulo Juan José
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb13852.x
Subject(s) - trypanosoma cruzi , polyclonal antibodies , biochemistry , antiserum , amastigote , cysteine , biology , microbiology and biotechnology , enzyme , proteinase 3 , proteinase k , cysteine proteinase inhibitors , blot , leishmania , antibody , parasite hosting , immunology , gene , apoptosis , caspase , programmed cell death , world wide web , computer science , autoantibody
Epinastigotes of different stocks of Trypanosoma cruzi contain levels of proteinase activity on azocasein; amastigotes and trypmastigotes contain 10‐fold lower levels of this proteolytic activity, which seems, therefore, to be developmentally regulated. The proteinase could be detected as a broad band, centered at about 60 kDa, which in some resolved into two close bands, in (a) SDS‐polyacrylamide gels containing fibrinogen, and (b) Western blots probed with polyclonal rabbit antiserum prepared against purified cystein proteinase. No proteinase activity was observed at molecular weights lower than 55 kDa. The results show that the enzyme preciously purified is teh major cysteine proteinase present in epimastigotes of all stocks of T. cruzi tested.