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An automated comprehensive ultrasens...

Michels, David A.

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An automated comprehensive ultrasensitive two-dimensional capillary electrophoresis system for proteomic analysis.

Record Type:	Electronic resources : Monograph/item
Title/Author:	An automated comprehensive ultrasensitive two-dimensional capillary electrophoresis system for proteomic analysis./
Author:	Michels, David A.
Description:	290 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1837.
Contained By:	Dissertation Abstracts International65-04B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3130863

An automated comprehensive ultrasensitive two-dimensional capillary electrophoresis system for proteomic analysis.
Michels, David A.

An automated comprehensive ultrasensitive two-dimensional capillary electrophoresis system for proteomic analysis. - 290 p.

Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1837.

Thesis (Ph.D.)--University of Washington, 2004.

Capillary electrophoresis (CE) coupled to a laser-induced fluorescence (LIF) sheath-flow cuvette detector offers a powerful method for analysis of a variety of biomolecules. CE-LIF generates high efficiencies and resolution, large peak capacities, and easily automated instrumentation. My thesis work demonstrates these parameters with one-dimensional (1-D) CE separations of Deinococcus radiodurans protein homogenates; my work also extends to the development of a comprehensive two-dimensional (2-D) system using hyphenated CE mechanisms.Subjects--Topical Terms:

586156
Chemistry, Analytical.

An automated comprehensive ultrasensitive two-dimensional capillary electrophoresis system for proteomic analysis.
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035 $a (UnM)AAI3130863
035 $a AAI3130863
040 $a UnM $c UnM
100 1 $a Michels, David A. $3 1949613
245 1 3 $a An automated comprehensive ultrasensitive two-dimensional capillary electrophoresis system for proteomic analysis.
300 $a 290 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1837.
500 $a Chair: Norman J. Dovichi.
502 $a Thesis (Ph.D.)--University of Washington, 2004.
520 $a Capillary electrophoresis (CE) coupled to a laser-induced fluorescence (LIF) sheath-flow cuvette detector offers a powerful method for analysis of a variety of biomolecules. CE-LIF generates high efficiencies and resolution, large peak capacities, and easily automated instrumentation. My thesis work demonstrates these parameters with one-dimensional (1-D) CE separations of Deinococcus radiodurans protein homogenates; my work also extends to the development of a comprehensive two-dimensional (2-D) system using hyphenated CE mechanisms.
520 $a D. radiodurans tetrads are lysed using mechanical stress with glass beads. Cytosolic and membrane-bound proteins from the bacteria are solublized and denatured in SDS-containing buffer at elevated temperatures. A fluorogenic dye, 3-(2-furoyl)-quinoline-2-carboxaldehyde (FQ), is reacted with SDS-proteins to form a highly fluorescent protein product.
520 $a Separations in the 1-D mode using sub-micellar capillary zone electrophoresis (CZE), micellar electrokinetic capillary chromatography (MECC), and capillary sieving electrophoresis (CSE) are used for the analysis of D. radiodurans protein homogenates. For all techniques, high efficient separations are obtained with peak capacities ranging between 100 and 140 for CZE and MECC separations. However, efficiencies for CSE are low and typically generate a peak capacity near 60.{09}The average standard deviations for CE separated FQ-labeled proteins from D. radiodurans are 1.3-seconds for CZE, 1.0-seconds for MECC, and 3.0-seconds for CSE. The predicted peak capacity for hyphenating CSE with CZE or MECC is nearly 7,000 spots.
520 $a Various combinations of 2-D CE-LIF are hyphenated for protein analysis of D. radiodurans: CZE x CZE, CZE x MECC, CSE x CZE, and CSE x MECC. The most impressive separations are obtained by coupling a low ionic strength sieving matrix in the CSE dimension with a micellar buffer containing 10- to 20-% organic modifiers in the MECC buffer. 2-D CSE x MECC separations generate a median standard deviation of 5.6-seconds for the CSE dimension and 2.3-seconds for the MECC dimension. In this combination, the total spot capacity is approximately 700, which is only 10-% of the predicted value. Losses are attributed to lengthy 2-D analysis times, diffusion of proteins in the CSE dimension, and short separation windows in the MECC dimension.*
520 $a *This dissertation is a compound document (contains both a paper copy and a CD as part of the dissertation). The CD requires the following system requirements: Microsoft Office; Windows MediaPlayer or RealPlayer.
590 $a School code: 0250.
650 4 $a Chemistry, Analytical. $3 586156
690 $a 0486
710 2 0 $a University of Washington. $3 545923
773 0 $t Dissertation Abstracts International $g 65-04B.
790 1 0 $a Dovichi, Norman J., $e advisor
790 $a 0250
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3130863