Regulatory effects of polyamines on membrane-bound acetylcholinesterase.
The effects of putrescene, spermidine and spermine on membrane-bound acetylcholinesterase from human erythrocyte ;ghosts' and the solubilized enzyme of the electric organ of the electric eel were studied by kinetic methods. Measurements were made by using a photometric method which made it possible to record the enzyme reaction in the steady-state phase. Substrate-concentration-dependent activation and inhibition of acetylcholinesterase by polyamines is similar to that by Na(+), K(+), Ca(2+), Mg(2+) and certain quaternary and bisquaternary amines. The kinetics suggest an allosteric reaction mechanism. On the basis of the kinetic results a role for the polyamines as modulators of synaptic acetylcholinesterase is proposed.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000494:Allosteric Regulation; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology*; D002800:Cholinesterase Inhibitors; D004557:Electric Organ / Q000201:enzymology; D004593:Electrophorus; D004789:Enzyme Activation; D004912:Erythrocytes / Q000201:enzymology; D006801:Humans; D007700:Kinetics; D011073:Polyamines / Q000494:pharmacology*; D011700:Putrescine / Q000494:pharmacology; D013095:Spermidine / Q000494:pharmacology; D013096:Spermine / Q000494:pharmacology
D002800:Cholinesterase Inhibitors; D011073:Polyamines; D013096:Spermine; D000110:Acetylcholinesterase; D013095:Spermidine; D011700:Putrescine