Binding properties of SH3 peptide ligands identified from phage-displayed random peptide libraries

In this work the effects of parathion (a competitive acetylcholinesterase inhibitory agent) on the enzyme activity was studied by cytochemical methods in the kidney of rats; being the doses used not inhibitory of red blood cells acetylcholinesterase (subtoxic dose). Two groups of rats were used: control (CR) and parathion-treated (TR) groups, both submitted to a water deprivation period of 24 h. for induction of primary thirst. The treated-rats group received parathion i.p. at doses of 600 micrograms/100g body weight. For demonstration of acetylcholinesterase activity, renal tissue incubation was performed by the Karnovsky and Roots method with the Tsuji Larabi variation. The results of the five assays of incubation enable us to conclude that there exists a noticeable activity of acetylcholinesterase in the renal cortex of control rats, which is blocked by subtoxic doses of organophosphorus pesticide. We suggest that the natriuretic effect of parathion can be explained by this mechanism.