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    Quantitation of the Noncovalent Cellular Retinol-Binding Protein, Type 1 Complex Through Native Mass Spectrometry

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    Author
    Li, W.
    Yu, J.
    Kane, M.A.
    Date
    2017
    Journal
    Journal of the American Society for Mass Spectrometry
    Publisher
    Springer New York LLC
    Type
    Article
    
    Metadata
    Show full item record
    See at
    https://doi.org/10.1007/s13361-016-1499-5
    Abstract
    Native 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.
    Sponsors
    This 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).
    Keyword
    Cellular retinol-binding protein
    Native mass spectrometry
    Noncovalent protein complex
    Quantification
    Vitamin A
    Identifier to cite or link to this item
    https://www.scopus.com/inward/record.uri?eid=2-s2.0-85006355611&doi=10.1007%2fs13361-016-1499-5&partnerID=40&md5=dc6a309c473acefbc1f321841fe1594e; http://hdl.handle.net/10713/11074
    ae974a485f413a2113503eed53cd6c53
    10.1007/s13361-016-1499-5
    Scopus Count
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    UMB Open Access Articles 2017

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