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dc.contributor.authorChen, Wei-Yuen_US
dc.contributor.authorChen, Yu-Chieen_US
dc.date.accessioned2014-12-08T15:15:41Z-
dc.date.available2014-12-08T15:15:41Z-
dc.date.issued2006-10-01en_US
dc.identifier.issn1618-2642en_US
dc.identifier.urihttp://dx.doi.org/10.1007/s00216-006-0427-0en_US
dc.identifier.urihttp://hdl.handle.net/11536/11713-
dc.description.abstractSilane-immobilized magnetic iron oxide particles were used as the assisting material in surface-assisted laser desorption/ionization (SALDI) mass spectrometric analysis. This approach can be used to analyze small proteins and peptides. The upper detectable mass range is approximately 16 kDa. The detection limit for peptides is about 20 fmol. Silanized iron oxide particles with negatively charged functionalities can also be used as the affinity probes to selectively trap oppositely charged species from sample solutions by adjusting the pH of the solution. A tryptic digest product of cytochrome C at a concentration as low as 10 nM can be enriched by the particles and directly analyzed by iron oxide SALDI MS without the need for elution steps. Affinity-based mass spectrometry using the bifunctional silanized magnetic iron oxide particles as the SALDI matrix and concentrating probe is demonstrated in this study.en_US
dc.language.isoen_USen_US
dc.subjectSALDI MSen_US
dc.subjectmagnetic nanoparticlesen_US
dc.subjectaffinity-based mass spectrometryen_US
dc.subjectaffinity probesen_US
dc.subjectinorganic matrixen_US
dc.titleAffinity-based mass spectrometry using magnetic iron oxide particles as the matrix and concentrating probes for SALDI MS analysis of peptides and proteinsen_US
dc.typeArticleen_US
dc.identifier.doi10.1007/s00216-006-0427-0en_US
dc.identifier.journalANALYTICAL AND BIOANALYTICAL CHEMISTRYen_US
dc.citation.volume386en_US
dc.citation.issue3en_US
dc.citation.spage699en_US
dc.citation.epage704en_US
dc.contributor.department應用化學系zh_TW
dc.contributor.department應用化學系分子科學碩博班zh_TW
dc.contributor.departmentDepartment of Applied Chemistryen_US
dc.contributor.departmentInstitute of Molecular scienceen_US
dc.identifier.wosnumberWOS:000240713500035-
dc.citation.woscount62-
Appears in Collections:Articles


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