Characterization of Seed Storage Proteins from Chickpea Using 2D Electrophoresis Coupled with Mass Spectrometry. (10th April 2016)

• Record Type: Journal Article
• Authors: Singh, Pramod Kumar; Shrivastava, Nidhi; Chaturvedi, Krishna; Sharma, Bechan; Bhagyawant, Sameer S.
• Other Names: Linhardt Robert J. Academic Editor.
• Is Part Of: Biochemistry research international. Volume 2016(2016)
• Publication Date: 2016-04-10
• Subjects: Biochemistry -- Periodicals; Biochemistry -- Research -- Periodicals; 572.05
• DOI: 10.1155/2016/1049462
• Languages: English
• ISSNs: 2090-2247

Abstract

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 .