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- W319778405 abstract "Publisher Summary This chapter discusses the chemical modification of protein method to identify essential groups in the acetylcholine receptors (AChR) of Limnaea stagnalis neurones and to reveal conformational transition at different functional states of the receptor. Essential groups of the AChRs of Limnaea stagnalis neurones were identified and conformational transitions of different receptor states were revealed, by the method of chemical modification of proteins with the help of the voltage-clamp technique. All the reagents used modified AChRs specifically. Experiments with carbodiimide, dithiothreitol (DTT) and SH-alkylating-agents showed: (1) there is a carboxyl group in the anionic subsite or near it, and an essential disulphide bond in the AChR molecule; (2) agonists induce a conformational transition of AChR, which masks the disulphide bond against DTT attack; (3) two different conformations of the desensitized AChR can exist depending on whether the active site is occupied by an agonist or free. In the former state, the disulphide bond is inaccessible to DTT. The high value of the Hill coefficient for responses to ACh and its lowering after treatment with P-halogenoethylamines suggest an oligomeric structure of Limnaea neurone AChRs and positive cooperativity between subunits." @default.
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- W319778405 date "1979-01-01" @default.
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- W319778405 title "Acetylcholine Receptor of Limnaea Stagnalis Neurones. Study of the Active Site Functional Groups" @default.
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- W319778405 doi "https://doi.org/10.1016/s0079-6123(08)64641-5" @default.
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