Studies on ali-esterases. 6. Selective inhibitors of the esterases of brain and saprophytic mycobacteria

Abstract

The ali-esterase activity of rat brain, Mycobacterium phlei and 3 other strains of Mycobacterium was determined manometrically using tributyrin as sub-strate following a 30 minute preincubation period at 37[degree]C with one of a series of 49 inhibitors, chiefly organophosphorous compounds and carbamate esters. Residual cholinesterase activity was measured using [beta]-methylcholine as substrate. Although many of the substances investigated were poor inhibitors of true cholinesterase some were highly effective against ali-esterases. No compound was found that would act as a selective inhibitor of the all esterases without inhibiting cholin-esterases.