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RESEARCH PRODUCT
Regulatory effects of polyamines on membrane-bound acetylcholinesterase
A. KossorotowH. U. WolfNikolaus Seilersubject
Reaction mechanismErythrocytesSpermidineKineticsAllosteric regulationSpermineBiochemistrychemistry.chemical_compoundAllosteric RegulationPolyaminesPutrescineAnimalsHumansMolecular Biologychemistry.chemical_classificationElectric OrganbiologyCellular Interactions and Control ProcessesCell MembraneCell Biologybiology.organism_classificationAcetylcholinesteraseElectric eelEnzyme ActivationSpermidineKineticsEnzymechemistryBiochemistryElectrophorusAcetylcholinesteraseSpermineCholinesterase Inhibitorsdescription
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+, Ca2+, Mg2+ 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1974-10-01 | Biochemical Journal |