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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Bromberg, Avraham Marx, Sharon Frishman, Gad |
| Description | Author Affiliation: Bromberg A ( Department of Physical Chemistry, Israel Institute for Biological Research, P. O. Box 19, Ness Ziona 74100, Israel. avraham.bromberg@gmail.com) |
| Abstract | The thermal inactivation of immobilized cholinesterase enzymes (ChE) in solid matrices where the protein unfolding is blocked was studied, thus enabling investigation of the kinetics of the inactivation process directly from the native structure to the inactivated state. The thermal inactivation of butyrylcholinesterase (BChE), recombinant human acetylcholinesterase (rHuAChE), and eel acetylcholinesterase (AChE) enzymes was studied in dry films composed of poly(vinyl pyrollidone) (PVP), bovine serum albumin (BSA) and trehalose at 60°–120 °C. The kinetics follows a bi-exponential decay equation representing a combination of fast and slow processes. The activation enthalpy Δ $H^{\\\#}$ and the activation entropy Δ $S^{\\\#}$ for each of the three enzymes have been evaluated. The values of Δ $H^{\\\#}$ for the fast process and for the slow process of BChE are 33 ± 3, and 28 ± 2 kcal/mol, respectively, and the values of Δ $S^{\\\#}$ are 0.84 ± 0.04, and − 18.2 ± 0.5 cal/deg, respectively. The appropriate value of Δ $H^{\\\#}$ for rHuAChE is 26 ± 2 Kcal/mol, for both processes and the values of Δ $S^{\\\#}$ are − 17.6 ± 0.9, and − 23.0 ± 0.9 cal/deg, respectively. Similarly, the values of Δ $H^{\\\#}$ for eelAChE are 30 ± 3, 31 ± 1 kcal/mol, and the values of Δ $S^{\\\#}$ are − 6.7 ± 0.5, − 9.1 ± 0.2 cal/deg respectively. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 6 |
| Volume Number | 1784 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2008-06-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Cholinesterases Chemistry Metabolism Enzymes, Immobilized Animals Butyrylcholinesterase Kinetics Temperature Time Factors Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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