Kinetic constants for the inhibition of camel retinal acetylcholinesterase by the carbamate insecticide lannate.
We have designed this study to determine various kinetic parameters of camel retinal membrane-bound acetylcholinesterase (AChE; EC 3.1.1.7) inhibition by carbamate insecticide lannate [methyl N-[[(methylamino)carbonyl]oxy] ethanimidothioate]. All these kinetic constants were derived by simple graphical methods. The value of kinetic parameters was estimated as follows: 0.061 microM)(-1), 1.14 (microM)(-1), 0.216 microM, 0.016 min(-1), 0.0741 (gammaM min)(-1) 0.746 microM, and 4.42 microM for velocity constant (Kv), new inhibition constant (Knic), dissociation constant (Kd), carbamylation rate constant (k2c), overall carbamylation rate constant (k'2), 50% inhibition constant (K150), and 99% inhibition constant (K199), respectively. These unique methods may be used to estimate such kinetic parameters for time-dependent inhibition of enzymes by variety of chemicals, insecticides, herbicides, and drugs.
Kamal
M A
MA
Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
Al-jafari
A A
AA
D000109:Acetylcholine / Q000378:metabolism*; D000818:Animals; D002162:Camelus / Q000378:metabolism*; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D007306:Insecticides / Q000494:pharmacology*; D007700:Kinetics; D008724:Methomyl / Q000494:pharmacology*; D012160:Retina / Q000201:enzymology*
D002800:Cholinesterase Inhibitors; D007306:Insecticides; D008724:Methomyl; D000109:Acetylcholine