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Biochemistry Research International
Volume 2016 (2016), Article ID 1049462, 6 pages
http://dx.doi.org/10.1155/2016/1049462
Research Article

Characterization of Seed Storage Proteins from Chickpea Using 2D Electrophoresis Coupled with Mass Spectrometry

1School of Studies in Biotechnology, Jiwaji University, Gwalior 474011, India
2Department of Bioscience & Biotechnology, Banasthali University, Banasthali 304022, India
3Defense Research & Development Establishment, Gwalior 474011, India
4Department of Biochemistry, University of Allahabad, Allahabad 211002, India

Received 21 November 2015; Revised 27 February 2016; Accepted 20 March 2016

Academic Editor: Robert J. Linhardt

Copyright © 2016 Pramod Kumar Singh 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.

Abstract

Proteomic analysis was employed to map the seed storage protein network in landrace and cultivated chickpea accessions. Protein extracts were separated by two-dimensional gel electrophoresis (2D-GE) across a broad range 3.0–10.0 immobilized pH gradient (IPG) strips. Comparative elucidation of differentially expressed proteins between two diverse geographically originated chickpea accessions was carried out using 2D-GE coupled with mass spectrometry. A total of 600 protein spots were detected in these accessions. In-gel protein expression patterns revealed three protein spots as upregulated and three other as downregulated. Using trypsin in-gel digestion, these differentially expressed proteins were identified by matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS) which showed 45% amino acid homology of chickpea seed storage proteins with Arabidopsis thaliana.