Brestkin_1986_Ukr.Biokhim.Zh_58_26

Alkyl tributylphosphonium and triphenylphosphonium derivatives as well as tetraphenylphosphonium were first studied as inhibitors of acetylcholinesterase of human blood erythrocytes and butyrylcholinesterase of horse blood serum. The inhibition is reversible, of mixed type, with a different contribution of competitive and uncompetitive components. The value of the inhibitory effect is essentially dependent on the structure of phosphonium compounds, especially in experiments with butyrylcholinesterase: allyltriphenylphosphonium is 290 times as strong enzyme inhibitor as methyltributylphosphonium. Hexyltributylphosphonium is identical to hexyltributylammonium in both the pattern and efficiency of the inhibitory action on cholinesterases.