Electrical excitability of artificial enzyme membranes. II. Electrochemical and enzyme properties of immobilized acetylcholinesterase membranes.
This paper deals with aspects of the reciprocal interaction between enzyme activity and the microenvironment or the potential difference in artificial proteinaceous membranes bearing cross-linked acetylcholinesterase. The potential difference resulting from asymmetric substrate injection into the system is recorded as a function of time. The influence of the membrane charge density on both enzyme activity and potential difference is studied by varying the external solution pH. The enzyme specific potential is initiated by local change of pH at the membrane level and the dependence on the buffer strength is studied. The recorded potential difference appears to be the result of the reciprocal interaction between enzyme reaction and the diffusion of substrate or products.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005780:Gelatin; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008564:Membrane Potentials; D008567:Membranes, Artificial; D012710:Serum Albumin, Bovine; D013552:Swine
D004800:Enzymes, Immobilized; D008567:Membranes, Artificial; D012710:Serum Albumin, Bovine; D005780:Gelatin; D000110:Acetylcholinesterase