Characterization of acetylcholinesterase purified from the lesser grain borer, Rhyzopertha dominica (Coleoptera: Bostrichidae).
Acetylcholinesterase (AChE, EC 3.1.1.7) purified from the lesser grain borer (Rhyzopertha dominica) was significantly inhibited by higher concentrations of the substrates acetylthiocholine (ATC), acetyl-(beta-methyl) thiocholine (A beta MTC) and propionylthiocholine (PTC). 2. The efficiency of AChE for hydrolyzing different substrates was ATC > A beta MTC > PTC > S-butyrylthiocholine. The enzyme activity was completely inhibited by 10(-5) M eserine or BW284C51, but was only partially inhibited by ethopropazine at the same concentration. These results confirmed that the purified enzyme was an typical insect AChE. 3. Non-denaturing and SDS polyacrylamide gel electrophoresis (PAGE) showed only one major molecular form in the purified AChE with a molecular weight of about 107,000 prior to reduction and about 56,000 after reduction, suggesting the homodimer of AChE linked with disulfide bonds.
Guedes
R N
RN
Departamento de Biologia Animal, Universidade Federal de Viçosa, Brasil.
Zhu
K Y
KY
Kambhampati
S
S
Dover
B A
BA
D000110:Acetylcholinesterase / Q000302:isolation & purification / Q000378:metabolism*; D000122:Acetylthiocholine / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D006868:Hydrolysis; D007313:Insecta / Q000201:enzymology*; D016622:Silver Staining; D013379:Substrate Specificity; D013860:Thiocholine / Q000031:analogs & derivatives / Q000378:metabolism / Q000494:pharmacology
D002800:Cholinesterase Inhibitors; C009063:propionylthiocholine; D000122:Acetylthiocholine; D013860:Thiocholine; D000110:Acetylcholinesterase