Alston_2020_J.Anesth.Hist_6_3

Irwin B. Wilson and anesthesiologist Richard J. Kitz found the enzyme acetylcholinesterase to be inactivated in two steps by covalently acting molecules resembling acetylcholine in structure. Such molecules rapidly and reversibly bind to the active site of the enzyme. Next, the reversible complex undergoes covalent fixation at a characteristic rate. The Kitz-Wilson phenomenon applies to many cases of time-dependent enzyme inhibition. Experimental data are commonly graphed in linear fashion on "Kitz-Wilson plots". Kitz also contributed to a gas chromatography-mass spectrometry assay for acetylcholine that was suitable for the nonbiological detection of that neurotransmitter in mammalian brain.