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 Vmax was 0.547 mumol/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 KI(intercept) were estimated to be 3.50 and 5.68 mmol/L, respectively. Ki was greater than K'i, indicating that CH has a greater binding affinity for the peripheral site than the active site.
journal_name
Cell Biol Toxicoljournal_title
Cell biology and toxicologyauthors
al-Jafari AA,Kamal MA,Alhomida ASdoi
10.1023/a:1007421124793subject
Has Abstractpub_date
1998-06-01 00:00:00pages
167-74issue
3eissn
0742-2091issn
1573-6822journal_volume
14pub_type
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