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Inhibition of butyrylcholinesterase (unknown origin)
Assay data:3 Tested
SummaryRelated BioAssays by Target
Inhibition of BChE (unknown origin) using BTCI as substrate preincubated for 15 min followed by substrate addition measured after 40 min by Ellman's method
Assay data:21 Tested
Inhibition of equine serum BuChE
Assay data:1 Tested
Inhibition of equine serum BuChE by Ellman's method
Assay data:21 Active, 14 Activity ≤ 1 µM, 22 Tested
Inhibition of human BuChE by Ellman's method
Assay data:1 Active, 1 Tested
Inhibition of equine serum BuChE at 10 uM by Ellman's method relative to control
Inhibition of equine serum BuChE assessed as residual enzyme activity at 50 uM using S-butyrylthiocholine iodide as substrate and measured for 60 secs by spectrophotometric analysis relative to control
Assay data:6 Tested
Competitive inhibition of equine serum BuChE assessed as Km of substrate using butyrylthiocholine iodide as substrate at 3XIC50 by Michaelis-Menten kinetics analysis (Rvb = 0.141 +/-0.011 mM)
Competitive inhibition of equine serum BuChE assessed as Km of substrate using butyrylthiocholine iodide as substrate at IC50 by Michaelis-Menten kinetics analysis (Rvb = 0.141 +/-0.011 mM)
Competitive inhibition of equine serum BuChE assessed as Km of substrate using butyrylthiocholine iodide as substrate at 1/2XIC50 by Michaelis-Menten kinetics analysis (Rvb = 0.141 +/-0.011 mM)
Competitive inhibition of equine serum BuChE assessed as Vmax of substrate using butyrylthiocholine iodide as substrate at 3XIC50 by Michaelis-Menten kinetics analysis (Rvb = 129 +/-4 10^-8 mol/s)
Irreversible inhibition of equine serum BuChE assessed as residual enzyme activity at IC50 using S-butyrylthiocholine iodide as substrate preincubated with enzyme for 60 mins followed by 80-fold dilution with BTC and DTNB and measured for 1 min by spectrophotometric analysis relative to control
Inhibition of equine serum BuChE assessed as residual enzyme activity at 10 uM using S-butyrylthiocholine iodide as substrate and measured for 60 secs by spectrophotometric analysis relative to control
Assay data:7 Tested
Inhibition of equine serum BuChE assessed as residual enzyme activity at 20 uM using S-butyrylthiocholine iodide as substrate and measured for 60 secs by spectrophotometric analysis relative to control
Competitive inhibition of equine serum BuChE assessed as Vmax of substrate using butyrylthiocholine iodide as substrate at 1/2XIC50 by Michaelis-Menten kinetics analysis (Rvb = 129 +/-4 10^-8 mol/s)
Competitive inhibition of equine serum BuChE assessed as Vmax of substrate using butyrylthiocholine iodide as substrate at IC50 by Michaelis-Menten kinetics analysis (Rvb = 129 +/-4 10^-8 mol/s)
Reversible inhibition of equine serum BuChE assessed as residual enzyme activity at IC50 using S-butyrylthiocholine iodide as substrate preincubated with enzyme for 60 mins followed by 80-fold dilution with BTC and DTNB and measured for 1 min by spectrophotometric analysis relative to control
Substrate activity at equine serum BuChE assessed as compound hydrolysis at 10XIC50 measured after 24 hrs by HPLC analysis
Assay data:12 Tested
Substrate activity at equine serum BuChE assessed as compound hydrolysis at 10XIC50 measured after 1 hr by HPLC analysis
Inhibition of equine serum BuChE using S-butyrylthiocholine iodide as substrate and measured for 60 secs by Ellman's method
Assay data:12 Active, 7 Activity ≤ 1 µM, 18 Tested
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