RT Journal Article
SR Electronic
T1 Conformational Changes of Acetylcholinesterase
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 104
OP 107
VO 4
IS 1
A1 KITZ, RICHARD J.
A1 KREMZNER, LEON T.
YR 1968
UL http://molpharm.aspetjournals.org/content/4/1/104.abstract
AB The conformation of highly purified acetylcholinesterase was measured with a spectropolarimeter. It was demonstrated that heat, strong base, a substrate, and anticholinesterase agents induce alterations in the conformation of this enzyme. ACKNOWLEDGMENT This study was supported in part by National Institutes of Health grants GM09069-05, NB 05184, and PH 446454; and National Science Foundation grant GB 5362.