5695
Sarah Adel Abd El-Ghany Abo El-Enin
Biochemical and toxicological studies on acetyl cholinesterase
from larvae of red palm weevil (Rhynchophorous ferrugineus)
Acetylcholinesterase (AChE), Detoxifying enzymes, R.
ferrugineus, Red palm weevil, Purification, Inhibition, Insecticides
Red palm weevil (RPW), Rhynchophorus ferrugineus, is the most destructive pest of many palm trees. The synthetic insecticides are the main strategy for control. Distribution of acetylcholinesterase (AChE), as a detoxifying enzyme and the target site of inhibition by insecticides, in different organs of the 10th instar larvae of the pest including whole gut, cuticle, fat body, head and haemolymph was estimated. The activity ranged from 314.9 to 3868 U/organ with specific activity ranged from 99 to 340.8 U/mg proteins where the cuticle had the highest enzyme level. The enzyme activity was tracked in cuticles during larval development; the11th instar larvae had the highest enzyme content with 5630 U/cuticle with specific activity 140 U/mg proteins. Two major AChE isoenzymes, AChEIIb and AChEIIIb, were purified by chromatography on ion exchange and gel filtration columns. The two isoenzymes AChEIIb and AChEIIIb had specific activities of 3504.3 and 2979 U/mg protein, molecular weights of 33 and 54 kDa, activation energies of 8.3 and 4.4 kCal/mol, respectively
2020
M.Sc
Cairo
Science