STABILIZATION OF DRY IMMOBILIZED ACETYLCHOLINESTERASE ON MICROTITRATION PLATES FOR COLORIMETRIC DETERMINATION OF ITS INHIBITORS IN WATER AND BIOLOGICAL-FLUIDS
Vk. Nguyen et al., STABILIZATION OF DRY IMMOBILIZED ACETYLCHOLINESTERASE ON MICROTITRATION PLATES FOR COLORIMETRIC DETERMINATION OF ITS INHIBITORS IN WATER AND BIOLOGICAL-FLUIDS, Enzyme and microbial technology, 20(1), 1997, pp. 18-23
The ability of the gelatin (or BSA)-trehalose film to convert normally
fragile dry immobilized acetylcholinesterase enzyme (AchE) into a sta
ble reagent is shown. The remarkable properties of the dry immobilized
AchE enzyme preparation are its stability to prolonged exposure to te
mperature as high as +50 degrees C and its tolerance to damages due to
acidic pH. The proposed method offers a rapid simple, and inexpensive
means for mass screening of AchE inhibitor residues such as pesticide
s and drugs in water, vegetables, and human blood serum. (C) 1997 by E
lsevier Science Inc.