From Glucose to Collagen: Characterization and Quantification of Biomolecules by Mass Spectrometry

Persistent Link:
http://hdl.handle.net/10150/193322
Title:
From Glucose to Collagen: Characterization and Quantification of Biomolecules by Mass Spectrometry
Author:
Jiang, Wei
Issue Date:
2008
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
A derivatization method is applied to chemically modify the glucose molecules. Then the derivatized C1 and C2 labeled glucose can be differentiated by tandem mass spectrometry. A multiple reaction monitoring method is developed to quantify the C1- and C2-13C labeled glucose, with deuterated glucose as the internal standard.Based on the fragmentation of cross-linked amino acids (pyridinoline (PYD) and deoxypyridinoline (DPD)), a precursor ion scan method is developed to detect DPD and PYD from a complex matrix. DPD is detected in a hydrolyzed mouse ventricle collagen sample by this method.A series of peptides and proteins are successfully ionized by a home made DESI source. The investigation of the sample surface effect shows that self assembled monolayer surfaces produce better signal than bare gold surfaces, implying that this is due to the lower electron transfer on SAM film which allows more ions to survive.
Type:
text; Electronic Thesis
Keywords:
mass spectrometry; glucose; collagen; DESI source
Degree Name:
MS
Degree Level:
masters
Degree Program:
Chemistry; Graduate College
Degree Grantor:
University of Arizona
Advisor:
Wysocki, Vicki H.
Committee Chair:
Wysocki, Vicki H.

Full metadata record

DC FieldValue Language
dc.language.isoENen_US
dc.titleFrom Glucose to Collagen: Characterization and Quantification of Biomolecules by Mass Spectrometryen_US
dc.creatorJiang, Weien_US
dc.contributor.authorJiang, Weien_US
dc.date.issued2008en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractA derivatization method is applied to chemically modify the glucose molecules. Then the derivatized C1 and C2 labeled glucose can be differentiated by tandem mass spectrometry. A multiple reaction monitoring method is developed to quantify the C1- and C2-13C labeled glucose, with deuterated glucose as the internal standard.Based on the fragmentation of cross-linked amino acids (pyridinoline (PYD) and deoxypyridinoline (DPD)), a precursor ion scan method is developed to detect DPD and PYD from a complex matrix. DPD is detected in a hydrolyzed mouse ventricle collagen sample by this method.A series of peptides and proteins are successfully ionized by a home made DESI source. The investigation of the sample surface effect shows that self assembled monolayer surfaces produce better signal than bare gold surfaces, implying that this is due to the lower electron transfer on SAM film which allows more ions to survive.en_US
dc.typetexten_US
dc.typeElectronic Thesisen_US
dc.subjectmass spectrometryen_US
dc.subjectglucoseen_US
dc.subjectcollagenen_US
dc.subjectDESI sourceen_US
thesis.degree.nameMSen_US
thesis.degree.levelmastersen_US
thesis.degree.disciplineChemistryen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorWysocki, Vicki H.en_US
dc.contributor.chairWysocki, Vicki H.en_US
dc.contributor.committeememberEvans, Dennisen_US
dc.contributor.committeememberOlenyuk, Bogdanen_US
dc.identifier.proquest2941en_US
dc.identifier.oclc659750564en_US
All Items in UA Campus Repository are protected by copyright, with all rights reserved, unless otherwise indicated.