Interaction between spin-labeled methacyne (I) and butyrylcholinesterase (BChE) was studied by ESR and enzyme kinetic methods. The compound (I) was shown to be a competitive reversible inhibitor, the value of Ki appeared to be 1.3 X 10(-5) M. Insertion of nitroxyl fragment in the methacyne molecule results in a two-fold increase of its inhibitory activity. The ESR spectrum of the enzyme-inhibitor complex was registered. This complex dissociates under the action of eserine, tetramethylammonium and hexamethonium. Scatchard plot reveals two different types of binding sites with Kdiss values 1.5 X 10(-5) M and 2.6 X 10(-4) M. One type of binding sites is identified as the enzyme active centre. The restricted motion of (I) in complex with BChE proves the assumption that the enzyme active centre is located in the split of macromolecule surface.
Dorokhov KE, Grigorian GL, Kardanov NA, Zhdanov RI, Trifonova SA (1985) [Interaction of spin-labeled methacyne analog with butyrylcholinesterase] Biofizika30: 23-6
Dorokhov KE, Grigorian GL, Kardanov NA, Zhdanov RI, Trifonova SA (1985) Biofizika30: 23-6