[Study of the molecular structure and mechanisms of pond snail neuron cholinoreceptor function by means of in vivo chemical modification].
The molecular structure of acetylcholine receptors (AChR) of Lymnaea stagnalis neurons has been studied using specific agents to definite chemical groups. The disulphide bond important for AChR function was discovered, the reduction of which by dithiotreitol (DTT) inactivates AChR. The drugs exciting AChR protect the disulphide bond against modification with DTT likely due to the conformational changes of an active site and its environment. Desensitized AChR can also be modified by DDT (if it is not occupied by agonist). It is suggested that the system transmitting the conformational change from the AChR active site to its ionophore is responsible for desensitization.
D000109:Acetylcholine / Q000494:pharmacology*; D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D004229:Dithiothreitol; D005724:Ganglia / Q000502:physiology*; D008195:Lymnaea / Q000502:physiology*; D010276:Parasympatholytics; D011487:Protein Conformation; D011950:Receptors, Cholinergic / Q000187:drug effects / Q000378:metabolism
D010276:Parasympatholytics; D011950:Receptors, Cholinergic; D000109:Acetylcholine; D004229:Dithiothreitol
Issledovanie molekuliarnoĭ struktury i mekhanizmov funktsionirovaniia kholinoretseptorov neĭronov prudovika s pomoshch'iu prizhiznennoĭ khimicheskoĭ modifikatsii.