Abstract
Immobilized metal affinity chromatography is a widely used method for the enrichment of phosphopeptides from proteolytic digests prior to mass spectrometric analysis. Here, we describe the selective enrichment of phosphopeptides from tryptic digests of proteins (α- and β-caseins) by zirconium phosphonate-magnetic Fe3O4/SiO2 (core/shell) nanoparticles for phosphoproteome analysis with MALDI-TOF mass spectrometry.
This chapter is based on an article that was published in J. Am. Soc. Mass Spectrom., 2008, 19, 1176–1186, L. Zhao, R. Wu, G. Han, H. Zhou, L. Ren, R. Tian, H. Zou, The Highly Selective Capture of Phosphopeptides by Zirconium Phosphonate-Modified Magnetic Nanoparticles for Phosphoproteome Analysis, copyright (2008), with permission from Elsevier. Hyper-text to the Elsevier homepage at http://www.elsevier.com.
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Acknowledgments
The authors acknowledge that this work was supported by the National Natural Science Foundation of China (No. 20875089), the National High Technology Research and Development Program of China (863 Program) (No. 2008AA02Z211), the Knowledge Innovation Program of Chinese Academy of Sciences (No. KSCX2-YW-G-046), and the Hundred Talent Program of the Chinese Academy of Sciences.
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Zhao, L., Wu, R., Zou, H. (2011). Selective Capture of Phosphopeptides by Zirconium Phosphonate-Magnetic Nanoparticles. In: Toms, S., Weil, R. (eds) Nanoproteomics. Methods in Molecular Biology, vol 790. Humana Press. https://doi.org/10.1007/978-1-61779-319-6_17
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DOI: https://doi.org/10.1007/978-1-61779-319-6_17
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