PT  - JOURNAL ARTICLE
AU  - GABOR KATO
TI  - Acetylcholinesterase
DP  - 1972 Sep 01
TA  - Molecular Pharmacology
PG  - 575--581
VI  - 8
IP  - 5
4099  - http://molpharm.aspetjournals.org/content/8/5/575.short
4100  - http://molpharm.aspetjournals.org/content/8/5/575.full
SO  - Mol Pharmacol1972 Sep 01; 8
AB  - A nuclear magnetic resonance method has been used to study the binding of atropine and eserine to purified squid acetylcholinesterase (EC 3.1.1.7). The dissociation constant, KD, and the linewidth of the acetylcholinesterase-inhibitor complex, Δνbound, for atropine and eserine were 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 eserine resulting from association with the enzyme. The results indicate that there is at least one binding site on the enzyme surface for atropine and one for eserine. Further evidence that the two sites are distinct is demonstrated by the fact that gallamine displaces atropine from its site without competing with eserine.