make a schematic diagram of BChE/AChE inhibitory determination Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide (AChI) molecules were utilized as substrate compounds of the reaction. In this regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) was used to estimate BChE/AChE activity. In summary, 100 μL Tris buffer solution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of the sample solution (50‐200 mL) were added in deionized water and also 20 μL of BChE/AChE enzymes solutions added. The mixture was then incubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and 25 mL) BChI/AChI were added to the incubator mixture. The reaction was also started by adding 50 μL BChI/AChI. The activity of these enzymes was evaluated using spectrophotometric spectra with a wavelength of 412 nm
make a schematic diagram of BChE/AChE inhibitory determination
Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide
(AChI) molecules were utilized as substrate compounds of the reaction. In
this regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) was
used to estimate BChE/AChE activity. In summary, 100 μL Tris buffer
solution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of the
sample solution (50‐200 mL) were added in deionized water and also
20 μL of BChE/AChE enzymes solutions added. The mixture was then
incubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and
25 mL) BChI/AChI were added to the incubator mixture. The reaction
was also started by adding 50 μL BChI/AChI. The activity of these
enzymes was evaluated using spectrophotometric spectra with a
wavelength of 412 nm.
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