[The peptidase site of butyrylcholinesterase is distinct from the esterase site].
Highly purified human plasma butyrylcholinesterase was inhibited by reversible inhibitors of esterase activity and modified by active-site-directed irreversible inhibitors of esterases and proteases. Peptidase and esterase activities of inhibited enzyme were simultaneously essayed from rates of hydrolysis of substance P (first cleavage) and butyrylthiocholine respectively. Inhibition parameters values and rates of inactivation of the two activities provide evidence that the peptidasic site is distinct from the esteratic site.
D001665:Binding Sites; D002091:Butyrylcholinesterase / Q000378:metabolism*; D002092:Butyrylthiocholine / Q000378:metabolism; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D002802:Cholinesterases / Q000378:metabolism*; D010450:Endopeptidases; D004950:Esterases; D006801:Humans; D066298:In Vitro Techniques; D013373:Substance P / Q000378:metabolism
D002800:Cholinesterase Inhibitors; D013373:Substance P; D002092:Butyrylthiocholine; D004950:Esterases; D002091:Butyrylcholinesterase; D002802:Cholinesterases; D010450:Endopeptidases
Le site peptidasique de la butyrylcholinestérase est distinct du site estérasique.