Table of Contents
International Journal of Proteomics
Volume 2011 (2011), Article ID 739615, 11 pages
http://dx.doi.org/10.1155/2011/739615
Research Article

Combined Use of a Solid-Phase Hexapeptide Ligand Library with Liquid Chromatography and Two-Dimensional Difference Gel Electrophoresis for Intact Plasma Proteomics

1Division of Pharmacoproteomics, National Cancer Center Research Institute, Chuo-ku, Tokyo 104-0045, Japan
2Laboratory of Genome Biology, Department of Biological Science and Technology, Tokyo University of Science, Tokyo 278-8510, Japan
3Laboratory of Proteome Research, National Institute of Biomedical Innovation, Osaka 567-0085, Japan

Received 2 May 2011; Accepted 9 June 2011

Academic Editor: David E. Misek

Copyright © 2011 Tatsuo Hagiwara et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Supplementary table 1: Recovery rate of protein samples after ProteoMiner treatment.

Supplementary table 2: Number of protein spots from fractionated plasma samples.

Supplementary table 3: Number of protein spots between the ProteoMiner-treated and untreated protein samples with different criteria.

Supplementary table 4: Number of protein spots observed by mass spectrometric protein identification.

Supplementary table 5: List of proteins identified by mass spectrometry.

Supplementary table 6: Detailed data of identified proteins.

Supplementary table 7: List of the identified proteins and their reported concentrations and references.

Supplementary figure 1: Reproducibility of protein fractionation by liquid chromatography. The ultraviolet detection (280 nm) trace for each run demonstrated consistent separation and fractionation. A. HiTrap Blue HP column; B. HiTrap Protein G HP column ; C. Resource Q column.

Supplementary figure 2: Two-dimensional difference gel electrophoresis images of ProteoMiner-treated and untreated protein samples. The ProteoMiner-treated and untreated samples were labeled with Cy5 and Cy3, respectively. A. original plasma; B. flow-through fraction of HiTrap Blue HP column; C. binding fraction of HiTrap Blue HP column; D. flow-through fraction of HiTrap Protein G HP column; E. binding fraction of HiTrap Protein G HP column; 0 mM fraction (F), 100 mM fraction (G), 150 mM (H), 200 mM (I), 250 mM (J), and 1 M fraction (K) of Resource Q column.

  1. Supplementary Material