Chen_1979_J.Pharm.Sci_68_1025

Reference

Title : Binding of mono- and bis-N-substituted benzoquinolinium halides to butyrylcholinesterase: fluorescence measurements - Chen_1979_J.Pharm.Sci_68_1025
Author(s) : Chen WS , Cocolas GH , Cavallito CJ
Ref : J Pharm Sci , 68 :1025 , 1979
Abstract :

The dissociation constants (Kdiss) of mono-and bis-N-substituted benzoquinolinium salts from butyrylcholinesterase were determined by the disappearance of the fluorescence of the free ligand. The Kdiss value determined by this method agreed closely with the dissociation constants (KI,s) of the free enzyme obtained by steady-state kinetic studies. The results indicate that the N-substituted benzoquinolinium salts with a strong binding ability to butyrylcholinesterase also are potent inhibitors of the esterolytic properties of the enzyme. Enzyme binding is favored by the coplanar structure and does not require a high concentration of charge on the onium function. The shape of the hydrophobic structures markedly influences binding.

PubMedSearch : Chen_1979_J.Pharm.Sci_68_1025
PubMedID: 480157

Related information

Citations formats

Chen WS, Cocolas GH, Cavallito CJ (1979)
Binding of mono- and bis-N-substituted benzoquinolinium halides to butyrylcholinesterase: fluorescence measurements
J Pharm Sci 68 :1025

Chen WS, Cocolas GH, Cavallito CJ (1979)
J Pharm Sci 68 :1025