Abstract
Activity and properties of cholinesterase fromAphelenchoides ritzema-boosi, a plant feeding nematode, were investigated by testing the reaction of the enzyme with different substrates and inhibitors. Butyrylthiocholine was a better substrate than propionyl- and acetylthiocholine. When compared with mammalian erythrocyte and plasma cholinesterase, the nematode enzyme was found to be extremely insensitive towards a number of well-known organophosphorus and carbamate inhibitors.

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