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

Biochemistry research international

Krishna Chaturvedi¹  Bechan Sharma²  Nidhi Shrivastava³  Pramod Kumar Singh⁴  Sameer S. Bhagyawant⁴ 

[1]Defense Research & Development Establishment, Gwalior 474011, India

[2]Department of Biochemistry, University of Allahabad, Allahabad 211002, India, allduniv.ac.in

[3]Department of Bioscience & Biotechnology, Banasthali University, Banasthali 304022, India, banasthali.org

[4]School of Studies in Biotechnology, Jiwaji University, Gwalior 474011, India, jiwaji.edu

DOI  :  10.1155/2016/1049462

学科分类：生物化学/生物物理

来源: Hindawi Publishing Corporation

【 摘 要 】

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.

【 授权许可】

CC BY