The fluorescence intensity of reversible inhibitor ethidium bromide fluorophore complex with equine blood butyryl cholinesterase decreases in the presence of inhibitor (tacrine) not fluorescing in the visible spectrum. An express method for tacrine evaluation is developed.

Fluorescence intensity of thioflavin T fluorogenic label increased significantly as a result of formation of enzyme-inhibitory complex with acetylcholinesterase of human blood erythrocytes. Thioflavin T is a reversible inhibitor, selectively reacting with acetylcholinesterase. Thioflavin T fluorescence intensity is proportional to acetylcholinesterase activity for the studied interval of enzyme activities. A rapid fluorescent method for measuring acetylcholinesterase activity is proposed.

Additionen der aus den Sulfoxiden (II) unter der Einwirkung von Li‐diisopropylamid entstehenden Anionen verlaufen regio‐ und stereospezifisch unter Bildung der trans‐1,4‐Addukte (III).

We present the results of spectral studies of the interactions between butyrylcholinesterase and ethidium bromide fluorophore inhibitor. The ethidium bromide fluorescence selectively increased in the presence of butyrylcholinesterase. A rapid method for evaluation of serum butyrylcholinesterase activity is developed.