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dc.contributor.authorLi, W.
dc.contributor.authorYu, J.
dc.contributor.authorKane, M.A.
dc.date.accessioned2019-10-08T19:43:49Z
dc.date.available2019-10-08T19:43:49Z
dc.date.issued2017
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85006355611&doi=10.1007%2fs13361-016-1499-5&partnerID=40&md5=dc6a309c473acefbc1f321841fe1594e
dc.identifier.urihttp://hdl.handle.net/10713/11074
dc.description.abstractNative mass spectrometry (MS) has become a valuable tool in probing noncovalent protein–ligand interactions in a sample-efficient way, yet the quantitative application potential of native MS has not been fully explored. Cellular retinol binding protein, type I (CrbpI) chaperones retinol and retinal in the cell, protecting them from nonspecific oxidation and delivering them to biosynthesis enzymes where the bound (holo-) and unbound (apo-) forms of CrbpI exert distinct biological functions. Using nanoelectrospray, we developed a native MS assay for probing apo- and holo-CrbpI abundance to facilitate exploring their biological functions in retinoid metabolism and signaling. The methods were developed on two platforms, an Orbitrap-based Thermo Exactive and a Q-IMS-TOF-based Waters Synapt G2S, where similar ion behaviors under optimized conditions were observed. Overall, our results suggested that within the working range (~1–10 μM), gas-phase ions in the native state linearly correspond to solution concentration and relative ion intensities of the apo- and holo-protein ions can linearly respond to the solution ratios, suggesting native MS is a viable tool for relative quantitation in this system.en_US
dc.description.sponsorshipThis project was funded with federal funds from NIH: R01HD077260 and NIH/NIAID contract no. HHSN272201000046C. Additional support was provided by the University of Maryland, School of Pharmacy, Mass Spectrometry Center (SOP1841-IQB2014).en_US
dc.description.urihttps://doi.org/10.1007/s13361-016-1499-5en_US
dc.language.isoen_USen_US
dc.publisherSpringer New York LLCen_US
dc.relation.ispartofJournal of the American Society for Mass Spectrometry
dc.subjectCellular retinol-binding proteinen_US
dc.subjectNative mass spectrometryen_US
dc.subjectNoncovalent protein complexen_US
dc.subjectQuantificationen_US
dc.subjectVitamin Aen_US
dc.titleQuantitation of the Noncovalent Cellular Retinol-Binding Protein, Type 1 Complex Through Native Mass Spectrometryen_US
dc.typeArticleen_US
dc.identifier.doi10.1007/s13361-016-1499-5
dc.identifier.pmid27709511


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