Title : Drugs-biomolecule interactions: binding study of substrate and inhibitors to acetylcholinesterase using NMR.

Pub. Date : 1975 Mar

PMID : 1151640






3 Functional Relationships(s)
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Protein Name
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1 NMR was used to study the binding of acetylcholine, atropine, and physostigmine to acetylcholinesterase. Atropine acetylcholinesterase (Cartwright blood group) Homo sapiens
2 The dissociation constant, KD and the linewidth of the acetylcholinesterase-inhibitor complex, increment v bound, for atropine and physostigmine can be estimated from the linewidth changes of the N-methyl and phenyl group resonances of atropine and from the N-methyl and C-methyl group resonances of physostigmine resulting from association with the enzyme. Atropine acetylcholinesterase (Cartwright blood group) Homo sapiens
3 The dissociation constant, KD and the linewidth of the acetylcholinesterase-inhibitor complex, increment v bound, for atropine and physostigmine can be estimated from the linewidth changes of the N-methyl and phenyl group resonances of atropine and from the N-methyl and C-methyl group resonances of physostigmine resulting from association with the enzyme. Atropine acetylcholinesterase (Cartwright blood group) Homo sapiens