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Development and application of biose...

Whelan, Rebecca Jean.

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Development and application of biosensor detectors.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Development and application of biosensor detectors./
作者:	Whelan, Rebecca Jean.
面頁冊數:	146 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1227.
Contained By:	Dissertation Abstracts International64-03B.
標題:	Chemistry, Analytical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3085240

Development and application of biosensor detectors.
Whelan, Rebecca Jean.

Development and application of biosensor detectors. - 146 p.

Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1227.

Thesis (Ph.D.)--Stanford University, 2003.

The ability to perform sensitive and selective detection of small amounts of protein is required in many applications. One approach to protein detection is affinity-based molecular recognition. We describe the development of a cell-based biosensor, the characterization of a commercial surface plasmon resonance (SPR) sensor, and the application of these detectors to cellular assays, detection of transient signals in analytical separations, and fundamental molecular physiology.Subjects--Topical Terms:

586156
Chemistry, Analytical.

Development and application of biosensor detectors.
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245 1 0 $a Development and application of biosensor detectors.
300 $a 146 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1227.
500 $a Adviser: Richard N. Zare.
502 $a Thesis (Ph.D.)--Stanford University, 2003.
520 $a The ability to perform sensitive and selective detection of small amounts of protein is required in many applications. One approach to protein detection is affinity-based molecular recognition. We describe the development of a cell-based biosensor, the characterization of a commercial surface plasmon resonance (SPR) sensor, and the application of these detectors to cellular assays, detection of transient signals in analytical separations, and fundamental molecular physiology.
520 $a We describe a novel single cell biosensor that uses antibodies to recognize proteins of interest. Antibodies are immobilized in the cell membrane by binding to endogenous receptors. Detection of protein antigens initiates cellular signal transduction cascades, resulting in a detectable rise in cytosolic Ca<super>2+</super>. This detection system is referred to as a single cell immunosensor. The use of antibodies confers to the single cell immunosensor flexibility and selectivity, and the cell's natural signal amplification confers sensitivity.
520 $a The loading and stimulation steps of the single cell immunosensor have been accomplished in a microfluidic device fabricated out of poly(dimethylsiloxane) (PDMS). A cell-trapping port and microfluidic delivery lines enable reproducible protein detection with more efficient consumption of time and reagents than the macroscale design.
520 $a A commercially available SPR sensor has been characterized for its ability to perform biological interaction analysis. Analytical figures of merit for the sensor are determined. Equilibrium dissociation constants for two important biomolecular interactions are determined and found to compare favorably with values reported in the literature and values determined in our laboratory by fluorescence correlation spectroscopy and surface fluorescence microscopy.
520 $a SPR has been used as a detector for capillary electrophoresis (CE). A mixture of high-refractive index solutions was resolved into its components and detected by an unmodified SPR sensing surface. Improvements in selectivity and sensitivity result from functionalizing the surface with proteins that recognize the molecule of interest. Nanoliter volumes of IgG have been delivered to the sensor electrophoretically and detected by SPR using a protein-A functionalized surface.
520 $a SPR has been used to develop procedures for immobilizing the β<sub> 2</sub> adrenergic receptor in a functional state. SPR studies were performed in parallel with fluorescence microscopy experiments that were sensitive to conformational changes in the receptor.
590 $a School code: 0212.
650 4 $a Chemistry, Analytical. $3 586156
650 4 $a Engineering, Biomedical. $3 1017684
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710 2 0 $a Stanford University. $3 754827
773 0 $t Dissertation Abstracts International $g 64-03B.
790 1 0 $a Zare, Richard N., $e advisor
790 $a 0212
791 $a Ph.D.
792 $a 2003
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