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Complex mixture analysis by matrix-a...

Wang, Michael Z.

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Complex mixture analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Complex mixture analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry./
Author:	Wang, Michael Z.
Description:	154 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2914.
Contained By:	Dissertation Abstracts International65-06B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3135147
ISBN:	049682371X

Complex mixture analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
Wang, Michael Z.

Complex mixture analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. - 154 p.

Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2914.

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

Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) has evolved as an important analytical tool for the analysis of peptides, proteins, nucleic acids, oligosaccharides and polymers. However, signal suppression effects complicate the MALDI-TOF MS analyses of complex mixtures. Protein expression profiling of either neat lung tumor cell lysate or neat serum from lung cancer patient by the MALDI-TOF MS only generated a small fraction (&sim;50 protein ion signals) of the total number of proteins that are expected to exist in either cell lysate or serum.

ISBN: 049682371XSubjects--Topical Terms:

586156
Chemistry, Analytical.

Complex mixture analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
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100 1 $a Wang, Michael Z. $3 1932750
245 1 0 $a Complex mixture analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
300 $a 154 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2914.
500 $a Supervisor: Michael C. Fitzgerald.
502 $a Thesis (Ph.D.)--Duke University, 2003.
520 $a Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) has evolved as an important analytical tool for the analysis of peptides, proteins, nucleic acids, oligosaccharides and polymers. However, signal suppression effects complicate the MALDI-TOF MS analyses of complex mixtures. Protein expression profiling of either neat lung tumor cell lysate or neat serum from lung cancer patient by the MALDI-TOF MS only generated a small fraction (&sim;50 protein ion signals) of the total number of proteins that are expected to exist in either cell lysate or serum.
520 $a In an attempt to understand the role of charge in defining the relative desorption/ionization efficiencies of peptides in a given mixture, several ionization tags were chemically attached to the N-termini of model peptides and their desorption/ionization behaviors during MALDI analysis were investigated. This work also describes a solid-phase sample preparation method for the MALDI-TOF MS analysis of a binary peptide mixture and a fractionation strategy that employs the liquid-phase isoelectric focusing technique. Both methods have been shown to reduce signal suppression effects during the MALDI analysis. Nearly 3-fold increase in the number of protein ions detected by the MALDI-TOF MS was observed for serum samples compared to when no pre-fractionation was employed. In total, about 148 unique protein ion signals were reproducibly detected in all 3 replicate fractionation trials.
520 $a Additionally, described here is a MALDI-TOF MS-based protein expression profiling strategy for the biomarker discovery for non-small cell lung cancer. Two proteins, MIF (macrophage migration inhibitory factor) and CypA (cyclophilin A) were identified as potential biomarkers in this work. Further investigation using a hydrogen/deuterium exchange-based technique unambiguously confirmed the protein identification for the biomarker, CypA. As part of this work, the dissociation constant for the CypA-CsA (cyclosporin A) complex was determined to be 32 +/- 20 nM. Our studies demonstrate that a MALDI-TOF MS based protein expression profiling can be used as an alternative strategy in the search for new diagnostic and therapeutic targets for lung cancer.
590 $a School code: 0066.
650 4 $a Chemistry, Analytical. $3 586156
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710 2 0 $a Duke University. $3 569686
773 0 $t Dissertation Abstracts International $g 65-06B.
790 1 0 $a Fitzgerald, Michael C., $e advisor
790 $a 0066
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3135147