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http://hdl.handle.net/2445/123187
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DC Field | Value | Language |
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dc.contributor.author | Peró Gascón, Roger | - |
dc.contributor.author | Pont Villanueva, Laura | - |
dc.contributor.author | Benavente Moreno, Fernando J. (Julián) | - |
dc.contributor.author | Barbosa Torralbo, José | - |
dc.contributor.author | Sanz Nebot, María Victoria | - |
dc.date.accessioned | 2018-06-21T14:04:35Z | - |
dc.date.available | 2018-06-21T14:04:35Z | - |
dc.date.issued | 2016 | - |
dc.identifier.issn | 0173-0835 | - |
dc.identifier.uri | http://hdl.handle.net/2445/123187 | - |
dc.description.abstract | In this paper, an on-line immunoaffinity solid-phase extraction capillary electrophoresis mass spectrometry (IA-SPE-CE-MS) method using magnetic beads (MBs) is described for the analysis of serum transthyretin (TTR), which is a protein related to different types of amyloidosis. First, purification of TTR from serum was investigated by off-line immunoprecipitation and CE-MS. The suitability of three Protein A (ProA) MBs (Protein A Ultrarapid AgaroseTM (UAPA), Dynabeads® Protein A (DyPA) and SiMAG-Protein A (SiPA)) and AffiAmino Ultrarapid AgaroseTM (UAAF) MBs to prepare an IA sorbent with a polyclonal antibody (Ab) against TTR, was studied. In all cases results were repeatable and it was possible the identification and the quantitation of the relative abundance of the 6 most abundant TTR proteoforms. Although recoveries were the best with UAPA MBs, UAAF MBs were preferred for on-line immunopurification because Ab was not eluted from the MBs. Under the optimised conditions with standards in IA-SPE-CE-MS, microcartridge lifetime (>20 analyses/day) and repeatability (2.9 and 4.3 % RSD for migration times and peak areas) were good, the method was linear between 5- 25 µg·mL-1 and limit of detection (LOD) was around 1 µg·mL-1 (25 times lower than by CE-MS, 25 µg·mL-1). A simple off-line sample pretreatment based on precipitation of the most abundant proteins with 5% (v/v) of phenol was necessary to clean-up serum samples. The potential of the on-line method to screen for familial amyloidotic polyneuropathy type I (FAP-I), which is the most common hereditary systemic amyloidosis, was demonstrated analysing serum samples from healthy controls and FAP-I patients. | - |
dc.format.extent | 12 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Wiley-VCH | - |
dc.relation.isformatof | Versió postprint del document publicat a: https://doi.org/10.1002/elps.201500495 | - |
dc.relation.ispartof | Electrophoresis, 2016, vol. 37, p. 1220-1231 | - |
dc.relation.uri | https://doi.org/10.1002/elps.201500495 | - |
dc.rights | (c) Wiley-VCH, 2016 | - |
dc.source | Articles publicats en revistes (Enginyeria Química i Química Analítica) | - |
dc.subject.classification | Electroforesi capil·lar | - |
dc.subject.classification | Espectrometria de masses | - |
dc.subject.classification | Camps magnètics | - |
dc.subject.other | Capillary electrophoresis | - |
dc.subject.other | Mass spectrometry | - |
dc.subject.other | Magnetic fields | - |
dc.title | Analysis of serum transthyretin by on-line immunoaffinity solid-phase extraction capillary electrophoresis mass spectrometry using magnetic beads | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/acceptedVersion | - |
dc.identifier.idgrec | 655669 | - |
dc.date.updated | 2018-06-21T14:04:36Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 26842820 | - |
Appears in Collections: | Articles publicats en revistes (Enginyeria Química i Química Analítica) |
Files in This Item:
File | Description | Size | Format | |
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655669.pdf | 1.04 MB | Adobe PDF | View/Open |
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