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Zr(IV)-immobilized Affinity Beads Prepared by Surface Template Polymerization for Capturing Phosphorylated Proteins

Published online by Cambridge University Press:  31 January 2011

Kazuya Uezu ,
Hidenobu Mizuki ,
Yudai Ito ,
Hisashi Harada  and
Haruka Oshiumi
Kazuya Uezu
Affiliation:
uezu@env.kitakyu-u.ac.jp, The University of Kitakyushu, Life and Environment Engineering, Kitakyushu, Japan
Hidenobu Mizuki
Affiliation:
d7610301@hibikino.ne.jp, The University of Kitakyushu, Life and Environment Engineering, Kitakyushu, Japan
Yudai Ito
Affiliation:
m08b0201@hibikino.ne.jp, The University of Kitakyushu, Life and Environment Engineering, Kitakyushu, Japan
Hisashi Harada
Affiliation:
m09b0601@hibikino.ne.jp, The University of Kitakyushu, Life and Environment Engineering, Kitakyushu, Japan
Haruka Oshiumi
Affiliation:
p0601501@hibikino.ne.jp, The University of Kitakyushu, Life and Environment Engineering, Kitakyushu, Japan
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Abstract

A novel immobilized metal affinity chromatography (IMAC) bead, Zr(IV)-immobilized resin, was prepared by surface template polymerization to enrich phosphorylated proteins and peptides from complex peptides mixtures. In order to enhance both the kinetics and the efficiency, large pathways for the proteins and peptides in the resin were formed, and the Zr(IV)-phosphate complexes were immobilized on the polymer surface. The morphology of the Zr(IV)-immobilized resin was evaluated the by measuring the specific surface area, pore volume, and pore distribution. The resin possessed large amount of the large-macro pores around 300 nm. The separation performance of β-casein from bovine serum albumin (BSA) solution was evaluated by phosphopeptide enrichment and MALDI-TOF MS analysis. The Zr(IV)-immobilized resin showed the high selectivity of the phosphopeptide.

Keywords

absorbentZrpurification
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1236: Symposium SS – Biosurfaces and Biointerfaces , 2009 , 1236-SS08-37
Copyright
Copyright © Materials Research Society 2010

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References

1 Feng, S. Ye, M. Zhou, H. Jiang, X. Jiang, X. Zou, H. Gong, B. Molecular & Cellular Proteomics, 6, 1656–1665(2007).Google Scholar
2 Nonglaton, G. Benitez, I. O. Guisle, I. Pipelier, M. Lger, J. Dubreuil, D. Tellier, C. Talham, D. R., Bujoli, B. J. Am. Chem. Soc 126, 1497–1502(2004).Google Scholar
3 Uezu, K. Nakamura, H. Goto, M. Murata, M. Maeda, M. Takagi, M. Nakashio, F. J. Chem.Eng. Jpn., 27, 436–438(1994).Google Scholar
4 Uezu, K. Nakamura, H. Kanno, J. Sugo, T. Goto, M. Nakashio, F. Macromolecules, 30, 3888–3891(1997).Google Scholar
5 Uezu, K. Kuwabara, T. Yoshida, M. Goto, M. Furusaki, S. Analy. Sci., 20, 1593–1597 (2004).Google Scholar
6 Meszarosova, K. Tishchenko, G. Bouchal, K. Bleha, M. React. Funct. Polym., 56, 27–35(2003).Google Scholar
7 Volkmann, A., Bruggemann, O. React. Funct. Polym., 66, 1725–1733(2006).Google Scholar