Binding sites on acetylcholinesterase and butyrylcholinesterase for pyridinium and imidazolium oximes, and other reversible ligands (CROSBI ID 77121)
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Reiner, Elsa ; Škrinjarić-Špoljar, Mira ; Simeon-Rudolf, Vera
engleski
Binding sites on acetylcholinesterase and butyrylcholinesterase for pyridinium and imidazolium oximes, and other reversible ligands
The paper deals with binding sites on acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) for reversible ligands. The purpose of the study was to establish whether there is evidence for an allosteric site on butyrylcholinesterase (BChE), and whether binding of a reversible ligand to the allosteric site can protect the catalytic site from phosphorylation by organophosphorus compounds. AChE and BChE activities were measured spectrophotometrically with acetylthiocholine or propionylthiocholine as substrates. From the kinetics of competition between substrates and reversible ligands (seven oximes and three ligands with no oxime group) it was suggested that BChE has a second binding site attributed to an allosteric site. The kinetics of enzyme protection showed that allosteric ligands can protect the catalytic site from phosphorylation.
acetylcholinesterase; butyrylcholinesterase; binding sites; inhibitors
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