Endogenous and rccombinant cruzipain, the major cysteine proteinase fr
om the protozoan parasite Trypanosoma cruzi, exhibit differences in th
e protein and circular dichroism spectra probably attributed to the ab
sence of the C-terminal domain in the recombinant enzyme. Substrate hy
drolysis of both molecules at 25 degrees C and neutral pH obeyed Micha
elis-Menten kinetics,whereas significant substrate inhibition was obse
rved above neutral pH. The results suggest that substrate inhibition o
f cruzipain is pH-dependent, and that the C-terminal domain does not p
lay an essential role in this process. (C) 1998 Federation of European
Biochemical Societies.