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G-quartet DNA stationary phases for capillary electrochromatographic separation of proteins

Record Type:	Electronic resources : Monograph/item
Title/Author:	G-quartet DNA stationary phases for capillary electrochromatographic separation of proteins
Author:	Silinski, Melanie Ann Rehder.
Description:	132 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5498.
Notes:	Supervisor: Linda B. McGown.
Contained By:	Dissertation Abstracts International64-11B.
Subject:	Chemistry, Analytical.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3111195
ISBN:	0496587250

G-quartet DNA stationary phases for capillary electrochromatographic separation of proteins
Silinski, Melanie Ann Rehder.

G-quartet DNA stationary phases for capillary electrochromatographic separation of proteins [electronic resource] - 132 p.

Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5498.

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

Separations of complex biological samples were performed to investigate the potential of the G-quartet DNA stationary phases for use in multi-dimensional proteomic analysis. Results demonstrate potential of this technique for identification of a unique biomarker in lung cancer, and for incorporation into a two-dimensional separation. With the ability to be directly interfaced with sensitive modes of detection and the demonstrated ability of the G-quartet DNA stationary phases to achieve rapid, reproducible, and possibly non-denaturing protein separations, this approach could prove valuable in both agriculture and the complex field of proteomics.

ISBN: 0496587250Subjects--Topical Terms:

224793
Chemistry, Analytical.

G-quartet DNA stationary phases for capillary electrochromatographic separation of proteins
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500 $a Source: Dissertation Abstracts International, Volume: 64-11, Section: B, page: 5498.
500 $a Supervisor: Linda B. McGown.
502 $a Thesis (Ph.D.)--Duke University, 2003.
520 # $a Separations of complex biological samples were performed to investigate the potential of the G-quartet DNA stationary phases for use in multi-dimensional proteomic analysis. Results demonstrate potential of this technique for identification of a unique biomarker in lung cancer, and for incorporation into a two-dimensional separation. With the ability to be directly interfaced with sensitive modes of detection and the demonstrated ability of the G-quartet DNA stationary phases to achieve rapid, reproducible, and possibly non-denaturing protein separations, this approach could prove valuable in both agriculture and the complex field of proteomics.
520 # $a Separations of two genetic variants of bovine beta-lactoglobulin, which differ by only two amino acid residues, were achieved using G-quartet stationary phases but not using either a bare capillary or a capillary coated with a non-G-quartet-forming oligonucleotide. Separation was also achieved using a capillary coated only with the linker molecule, but very strong protein-linker interactions were observed. These results suggest that the G-quartet stationary phases may result in less denaturing separation than is commonly achieved using hydrocarbon-based stationary phases.
520 # $a The development of automated processes that provide sensitive, rapid, and non-denaturing separations of a wide variety of proteins is becoming increasingly important in agriculture, industry, and medicine. Towards this end, G-quartet-forming oligonucleotides were investigated as stationary phases for protein separations by open-tubular capillary electrochromatography (OTCEC). A variety of protein systems, including bovine milk proteins, human cell lysates, and human serum, were utilized to study the potential of these novel stationary phases.
520 # $a The eight major proteins in bovine milk were also separated using this approach, without the traditional, harsh sample pre-treatments. Better resolution was achieved using the G-quartet-coated capillaries than was achieved using either a bare capillary or a non-G-quartet-forming oligonucleotide-coated capillary. A four-plane G-quartet stationary phase was able to resolve three peaks for alpha-casein, attributed to alphas2-casein and two genetic variants of alphas1-casein. It was also possible to detect thermal denaturation of the proteins in the milk sample using the four-plane G-quartet stationary phase. These results suggest that the G-quartet stationary phases could be used to separate very similar protein structures, such as those arising from genetic variations or post-translational modifications.
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773 0 # $g 64-11B. $t Dissertation Abstracts International
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790 1 0 $a McGown, Linda B., $e advisor
791 $a Ph.D.
792 $a 2003
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