کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1176391 961848 2008 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Microcalorimetric study of the inhibition of butyrylcholinesterase by carbamates
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Microcalorimetric study of the inhibition of butyrylcholinesterase by carbamates
چکیده انگلیسی

The inhibition of horse serum butyrylcholinesterase (EC 3.1.1.8) by three carbamates (eserine, neostigmine, and rivastigmine) was studied by flow microcalorimetry at 37 °C in Tris buffer (pH 7.5). The kinetics of carbamylation was studied in the absence or presence of the substrate, butyrylcholine, using an extension of the model described by Stojan and coworkers (FEBS Lett. 440 (1998) 85–88). The model was fitted to the data by a nonlinear regression procedure using simulated annealing followed by Marquardt’s method. The affinity of the carbamates for the free enzyme increased in the order neostigmine < eserine < rivastigmine, whereas the carbamylation rates followed an inverse order. In the case of rivastigmine, the results suggested that an acyl-enzyme–inhibitor complex could be formed either by reversible binding of the carbamate to the acyl-enzyme or by acylation of the enzyme–inhibitor complex. This work confirms the usefulness of microcalorimetry to study irreversible or progressive inhibitors and emphasizes the need to investigate the binding of such compounds to intermediate enzyme forms.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Analytical Biochemistry - Volume 373, Issue 2, 15 February 2008, Pages 247–252
نویسندگان
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