The NADP-linked glutamate dehydrogenase purified from epimastigotes of Trypanosoma cruzi was strongly, but not completely, inhibited by sulfhydryl reagents, in the presence of Tris-HCl or phosphate buffers. 2. The enzyme modified by preincubation with o-iodosobenzoate had a kinetic behaviour different from that shown by the enzyme modified with other inhibitors, such as N-ethylmaleimide or p-chloromercuribenzoate. 3. The inhibition by o-iodosobenzoate was additive with the inhibition by the other reagents tested. 4. It is suggested that two or more different sulfhydryl groups, placed probably near the active site, are involved in these effects.