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Effect of sevin on kinetic parameters of camel retina acetylcholinesterase
Author(s) -
Kamal Mohammad Amjad
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700202621
Subject(s) - acetylcholinesterase , chemistry , aché , michaelis–menten kinetics , carbaryl , enzyme kinetics , turnover number , hydrolysis , iodide , chromatography , stereochemistry , enzyme , enzyme assay , biochemistry , pesticide , biology , active site , inorganic chemistry , ecology
The present investigation addresses the effect of sevin (insecticide) on kinetic parameters of camel retina membrane‐bound acetylcholinesterase (AChE, EC 3.1.1.7). The Michaelis‐Menten constant (Ks) for the hydrolysis of acetylthiocholine iodide (ASCh) by AChE was 0.072 mM in the control system, a value decreased by 38‐55% in the sevin treated systems. The Vmax was 0.967 μmole/min/mg protein for the control system while it was decreased by 50‐84% in the sevin treated systems. The Lineweaver‐Burk plot, Dixon plot, and their secondary replots indicated that the nature of the inhibition was of the linear mixed type, i.e. uncompetitive and noncompetitive. The values of Ki(slope) and KI(intercept) were estimated as 6.194 and 2.811 μM, respectively. The turnover number (Kcat) and specificity constant (Ksp) were 74.65 min‐1 and 10.37×105 (M. min)‐1 in the control system respectively, while the values for both parameters were significantly decreased in the sevin treated systems.