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אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
Sol - Gel-Entrapped Cholinesterases: A Microtiter Plate Method for Monitoring Anti-cholinesterase Compounds
Year:
1998
Authors :
אהרונסון, נדב
;
.
אלטשטיין, מרים
;
.
בן-עזיז, אורנה
;
.
טורניאנסקי, אבנר
;
.
שגב, גלית
;
.
Volume :
46
Co-Authors:
Altstein, M., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel, Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Segev, G., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Aharonson, N., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Ben-Aziz, O., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Turniansky, A., Institute of Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Avnir, D., Institute of Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel, Department of Organic Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Facilitators :
From page:
3318
To page:
3324
(
Total pages:
7
)
Abstract:
Herein is reported the successful entrapment of three esterase enzymes within silica, by means of the sol - gel process. The enzymes were acetylcholinesterase (AChE) from electric eel (ee), AChE from bovine erythrocytes (er), and butyrylcholinesterase (BChE) from horse serum. Enzyme entrapment was carried out in a novel configuration by casting the doped sol - gel material in 96-well microtiter plates. The study determined the apparent kinetics of the activity and inhibition of the three entrapped enzymes and elucidated the optimal sol - gel matrix composition and preparation procedure. The enzyme mode of action within the sol - gel matrix was compared with that obtained in solution, under various experimental conditions. The activity of entrapped ee-AChE was found to depend on the concentration of the entrapped enzyme and on the sol - gel preparation procedure and composition. It was found that whereas the activity of ee-AChE was 3-4-times lower than that in solution, one gained significantly higher stability. The entrapped enzymes were sensitive to various organophosphates and to the carbamate carbaryl, with inhibition patterns similar to those obtained in aqueous reactions.
Note:
Related Files :
Carbamates
Cholinesterases
ORGANOPHOSPHATES
Residue analysis
Sol - Gel
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
20425
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:36
Scientific Publication
Sol - Gel-Entrapped Cholinesterases: A Microtiter Plate Method for Monitoring Anti-cholinesterase Compounds
46
Altstein, M., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel, Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Segev, G., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Aharonson, N., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Ben-Aziz, O., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Turniansky, A., Institute of Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Avnir, D., Institute of Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel, Department of Organic Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Sol - Gel-Entrapped Cholinesterases: A Microtiter Plate Method for Monitoring Anti-cholinesterase Compounds
Herein is reported the successful entrapment of three esterase enzymes within silica, by means of the sol - gel process. The enzymes were acetylcholinesterase (AChE) from electric eel (ee), AChE from bovine erythrocytes (er), and butyrylcholinesterase (BChE) from horse serum. Enzyme entrapment was carried out in a novel configuration by casting the doped sol - gel material in 96-well microtiter plates. The study determined the apparent kinetics of the activity and inhibition of the three entrapped enzymes and elucidated the optimal sol - gel matrix composition and preparation procedure. The enzyme mode of action within the sol - gel matrix was compared with that obtained in solution, under various experimental conditions. The activity of entrapped ee-AChE was found to depend on the concentration of the entrapped enzyme and on the sol - gel preparation procedure and composition. It was found that whereas the activity of ee-AChE was 3-4-times lower than that in solution, one gained significantly higher stability. The entrapped enzymes were sensitive to various organophosphates and to the carbamate carbaryl, with inhibition patterns similar to those obtained in aqueous reactions.
Scientific Publication
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