1. Large-scale speciation of selenium in rice proteins using ICP-MS assisted electrospray MS/MS proteomics
- Author
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Juliusz Bianga, Joanna Szpunar, Pracha Cheajesadagul, Carine Arnaudguilhem, Ryszard Lobinski, Institut des sciences analytiques et de physico-chimie pour l'environnement et les materiaux (IPREM), and Université de Pau et des Pays de l'Adour (UPPA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
Proteomics ,Spectrometry, Mass, Electrospray Ionization ,Electrospray ,Globulin ,Molecular Sequence Data ,Biophysics ,chemistry.chemical_element ,01 natural sciences ,Biochemistry ,Biomaterials ,Selenium ,03 medical and health sciences ,chemistry.chemical_compound ,Tandem Mass Spectrometry ,[CHIM]Chemical Sciences ,Storage protein ,Electrophoresis, Gel, Two-Dimensional ,Amino Acid Sequence ,Selenomethionine ,Shotgun proteomics ,Chromatography, High Pressure Liquid ,Plant Proteins ,030304 developmental biology ,2. Zero hunger ,chemistry.chemical_classification ,0303 health sciences ,Chromatography ,Two-dimensional gel electrophoresis ,Selenocysteine ,biology ,010401 analytical chemistry ,Metals and Alloys ,food and beverages ,Oryza ,0104 chemical sciences ,chemistry ,Chemistry (miscellaneous) ,biology.protein - Abstract
International audience; A Se-targeted bottom-up proteomics approach was developed for the identification of Se-containing proteins in rice grown naturally on seleniferous soils. The proteins were separated by 2D gel electrophoresis. The position of Se-containing spots was tentatively identified by the correlation between the 1D isoelectrofocusing (IEF) and 1D SDS electropherograms of a sample aliquot and confirmed by 78Se imaging in the 2D gel. The method was complemented by the ICP-MS assisted shotgun proteomics approach. The proteins were identified by capHPLC with the dual ICP MS and electrospray Orbitrap MS detection. The first ever comprehensive study of rice selenoproteome revealed the presence of selenium, as both selenomethionine (SeMet) and selenocysteine (SeCys) residues, in a dozen proteins including a 19 kDa globulin, granule-bound starch synthase, and the family of glutelin-type seed storage proteins.
- Published
- 2014
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