Highly cooperative inhibition of acetylcholinesterase by pentachlorophenol in human erythrocytes.
Pentachlorophenol (PCP) inhibited acetylcholinesterase (AchE) activity in human erythrocyte membranes with high cooperativity. The Hill coefficient for the inhibition was 4-5 in "untreated" membranes. Differences in the temperature (13, 25 and 37 degrees) or treatment with 1% Triton X-100 did not clearly affect the cooperativity which, however, increased after the erythrocyte membranes were treated with 2-mercaptoethanol and iodoacetatic acid, suggesting that higher cooperativity in the inhibition of AchE by PCP may reflect conformational changes of AchE. Thus, PCP may be useful for the study of AchE in human erythrocytes.
Igisu
H
H
Department of Environmental Toxicology, University of Occupational and Environmental Health, Kitakyushu, Japan.
Hamasaki
N
N
Ikeda
M
M
D000110:Acetylcholinesterase / Q000378:metabolism*; D000122:Acetylthiocholine / Q000378:metabolism; D002800:Cholinesterase Inhibitors / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000201:enzymology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007461:Iodoacetates; D019807:Iodoacetic Acid; D008297:Male; D008623:Mercaptoethanol; D010416:Pentachlorophenol / Q000494:pharmacology*; D013696:Temperature
D002800:Cholinesterase Inhibitors; D007461:Iodoacetates; D000122:Acetylthiocholine; D008623:Mercaptoethanol; D010416:Pentachlorophenol; D000110:Acetylcholinesterase; D019807:Iodoacetic Acid