ISSN:
1573-6822
Keywords:
acetylcholinesterase
;
cycloheximide
;
inhibition
;
kinetics
;
retina
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Abstract The kinetic parameters of inhibition of camel retinal acetylcholinesterase (AChE) activity by cycloheximide (CH) were investigated. For the control system, the Michaelis–Menten constant (K m)for the hydrolysis of acetylthiocholine iodide was found to be 0.076 mmol/L and the V max was 0.547 μmol/min per mg protein. In contrast, these parameters were decreased in the CH-treated systems. Dixon and Lineweaver–Burk plots, and their secondary replots, indicated that the inhibition was of the linear mixed type, which seems to be a combination of partial competitive and pure noncompetitive inhibition. The values of K′i(slope) and K I(intercept) were estimated to be 3.50 and 5.68 mmol/L, respectively. K i was greater than K′i, indicating that CH has a greater binding affinity for the peripheral site than the active site.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1007421124793
