Stability of membrane acetylcholinesterase in human erythrocytes treated with tetraphenylboron.
Treatment of human erythrocytes with non-hemolytic concentrations of tetraphenylboron causes irreversible inactivation of acetylcholinesterase, an enzyme located at or near the outer cell surface. By contrast to other agents which also inactivate acetylcholinesterase activity such as 1,5-difluoro-2,4-dinitrobenzene and glutaraldehyde, tetraphenylboron does not affect the thermostability of the enzyme, alter its susceptibility to denaturation by urea or hinder the proteolytic digestion of the erythrocyte membrane.
D000110:Acetylcholinesterase / Q000097:blood*; D001896:Boron Compounds / Q000494:pharmacology*; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D004355:Drug Stability; D004912:Erythrocytes / Q000187:drug effects / Q000201:enzymology*; D006358:Hot Temperature; D006801:Humans; D013775:Tetraphenylborate / Q000494:pharmacology*; D014508:Urea / Q000494:pharmacology
D001896:Boron Compounds; D013775:Tetraphenylborate; D014508:Urea; D000110:Acetylcholinesterase