Abstract：
:Using electric eel acetylcholinesterase (AChE) which was either membrane-bound (AChEm) or solubilized (AChEs), similar kinetics were seen in the absence of inhibitor or in the presence of edrophonium, trimethylammonium ion or paraoxon. Thus, both forms of the enzyme appear to behave similarly toward various inhibitors. However, in the presence of a probe sensitive to allosteric effects or changes in membrane fluidity, the two forms exhibit altered behavior. In the presence of F-, the relative rate of substrate hydrolysis by AChEm was reduced more rapidly than with AChEs, whether or not paraoxon was present. When inhibition by paraoxon (10(-7)-10(-4) M) was studied in the presence of F-, AChEs had a Hill coefficient of 1.0, whereas with AChEm the Hill coefficient changed from 0.8 to 1.5.
journal_name
Life Scijournal_title
Life sciencesauthors
Lenz DE,Maxwell DM,Walden MBdoi
10.1016/0024-3205(84)90593-9subject
Has Abstractpub_date
1984-01-16 00:00:00pages
219-24issue
3eissn
0024-3205issn
1879-0631pii
0024-3205(84)90593-9journal_volume
34pub_type
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