STABILIZATION OF DRY IMMOBILIZED ACETYLCHOLINESTERASE ON NITROCELLULOSE MEMBRANE FOR RAPID COLORIMETRIC SCREENING OF ITS INHIBITORS IN WATER AND BIOLOGICAL-FLUIDS
Vk. Nguyen et al., STABILIZATION OF DRY IMMOBILIZED ACETYLCHOLINESTERASE ON NITROCELLULOSE MEMBRANE FOR RAPID COLORIMETRIC SCREENING OF ITS INHIBITORS IN WATER AND BIOLOGICAL-FLUIDS, Analytical letters, 31(14), 1998, pp. 2457-2473
We show the ability of a gelatin and a BSA-trehalose film to convert n
ormally fragile dry immobilized acetylcholinesterase enzyme (AchE) int
o a stable reagent on nitrocellulose membrane. The remarkable property
of the dry immobilized AchE enzyme preparation is its stability when
exposed to temperatures as high as 50 degrees C. The proposed method o
ffers a rapid, simple, and inexpensive means in a non-laboratory setup
for qualitative analytical colorimetric screening of AchE inhibitor r
esidues such as pesticides and drugs in water and biological fluids.