| Abstract: | Membrane proteins have been isolated from neuromuscular synapses of the crab Potamon transcaspicum using a specific blocker of glutamatergic synapses, the neurotoxin of the spider Argiope lobata. These membrane components have been shown to induce glutamate-sensitive conductance in bilayer lipid membranes (BLM) in the presence of sodium ions. As an agent blocking desensitization of glutamatergic synapses, concanavalin A was shown to enhance the conductance and to abolish desensitization. Diethylester of glutamic acid as a blocker of glutamatergic synapses inhibited glutamate-induced conductance. No similar change in conductance was seen when BLM was modified by a membrane proteins -neurotoxin complex. Conductance current fluctuations induced by these receptor protein components were monitored by the single-channel registration method. |
