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פותח על ידי קלירמאש פתרונות בע"מ -
Sol-Gel Matrixes Doped with Atrazine Antibodies: Atrazine Binding Properties
Year:
1997
Source of publication :
Chemistry of Materials
Authors :
אהרונסון, נדב
;
.
אלטשטיין, מרים
;
.
ברונשטיין, אליסה
;
.
Volume :
9
Co-Authors:
Bronshtein, A., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Aharonson, N., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Avnir, D., Institute of Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Turniansky, A., Institute of Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Altstein, M., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel, Dept. of Entomology, Volcani Center, Bet Dagan 50250, Israel
Facilitators :
From page:
2632
To page:
2639
(
Total pages:
8
)
Abstract:
Sol-gel materials with antibody properties are described. These were constructed by the entrapment of monoclonal anti-atrazine antibodies (Mabs) in SiO2 sol-gel derived matrixes, which successfully recognized and bound atrazine, a widely used herbicide. The binding properties for atrazine were evaluated by comparing sol-gel entrapped anti-atrazine hybridoma culture fluids with entrapped purified immunoglobulins (IgGs). In the study, 14C-labeled and unlabeled atrazine, which are stable to hydrolysis or to other chemical decay processes, were used as analytes. Leaching of the antibodies was found to be zero. Stability was tested under various storage conditions and was found to be 100% for at least 2 months at room temperature, compared with a drop of 40% in solution. The response time was found not to differ considerably from that obtained in solution. Other factors tested included reproducibility of binding, dose response, nonspecific physisorption of atrazine to the ceramic matrix, and elution recoveries of atrazine from the doped sol-gel columns. An advantage of the sol-gel methodology is the elimination of the need to purify the IgGs from the Mab hybridoma culture fluids.
Note:
Related Files :
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תוכן קשור
More details
DOI :
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
29096
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:44
Scientific Publication
Sol-Gel Matrixes Doped with Atrazine Antibodies: Atrazine Binding Properties
9
Bronshtein, A., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Aharonson, N., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel
Avnir, D., Institute of Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Turniansky, A., Institute of Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel
Altstein, M., Institute of Plant Protection, Volcani Center, Bet Dagan 50250, Israel, Dept. of Entomology, Volcani Center, Bet Dagan 50250, Israel
Sol-Gel Matrixes Doped with Atrazine Antibodies: Atrazine Binding Properties
Sol-gel materials with antibody properties are described. These were constructed by the entrapment of monoclonal anti-atrazine antibodies (Mabs) in SiO2 sol-gel derived matrixes, which successfully recognized and bound atrazine, a widely used herbicide. The binding properties for atrazine were evaluated by comparing sol-gel entrapped anti-atrazine hybridoma culture fluids with entrapped purified immunoglobulins (IgGs). In the study, 14C-labeled and unlabeled atrazine, which are stable to hydrolysis or to other chemical decay processes, were used as analytes. Leaching of the antibodies was found to be zero. Stability was tested under various storage conditions and was found to be 100% for at least 2 months at room temperature, compared with a drop of 40% in solution. The response time was found not to differ considerably from that obtained in solution. Other factors tested included reproducibility of binding, dose response, nonspecific physisorption of atrazine to the ceramic matrix, and elution recoveries of atrazine from the doped sol-gel columns. An advantage of the sol-gel methodology is the elimination of the need to purify the IgGs from the Mab hybridoma culture fluids.
Scientific Publication
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