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• W1987185720 endingPage "3764" @default.
• W1987185720 startingPage "3759" @default.
• W1987185720 abstract "DNA aptamers that form a G-quartet conformation were covalently attached to a capillary surface for open-tubular capillary electrochromatographic separation of bovine β-lactoglobulin variants A and B, which vary by 2 of their 162 amino acid residues. Separation was achieved using a 4-plane, G-quartet aptamer stationary phase with tris(hydroxymethyl)aminomethane (Tris) or phosphate buffer as the mobile phase. In control experiments, separation did not occur using either an oligonucleotide of similar base composition but which does not form a G-quartet structure, or using capillary zone electrophoresis on a bare capillary under similar experimental conditions. Separation was achieved using a capillary coated only with the covalent linker molecule. In phosphate buffer, the separations were similar for aptamer-coated and linker-only stationary phases, while in Tris buffer, retention times were almost doubled for the linker-only capillary. When Tris buffer is the mobile phase, there appears to be weaker interactions between the proteins and the stationary phase that may result in a gentler, less denaturing separation than is commonly achieved using hydrocarbon-based stationary phases." @default.
• W1987185720 created "2016-06-24" @default.
• W1987185720 creator A5043742872 @default.
• W1987185720 creator A5073595754 @default.
• W1987185720 date "2001-09-01" @default.
• W1987185720 modified "2023-10-16" @default.
• W1987185720 title "Open-tubular capillary electrochromatography of bovine β-lactoglobulin variants A and B using an aptamer stationary phase" @default.
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• W1987185720 doi "https://doi.org/10.1002/1522-2683(200109)22:17<3759::aid-elps3759>3.0.co;2-c" @default.
• W1987185720 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11699915" @default.
• W1987185720 hasPublicationYear "2001" @default.
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