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A metallomics approach discovers selenium-containing proteins in selenium-enriched soybean.
1Department of Chemistry, University of Cincinnati, Cincinnati, OH 45221-0172, USA.
Analytical and Bioanalytical Chemistry
|March 30, 2012
Summary
High-molecular-weight selenium (Se) species dominate Se in soybean beans. This study identified Se-containing proteins, including Bowman-Birk proteinase isoinhibitor, in Se-enriched soybeans using advanced metallomics techniques.
Area of Science:
- Biochemistry
- Plant Science
- Metallomics
Background:
- Previous research indicated high-molecular-weight selenium (Se) species constitute 82% of total Se in Se-enriched soybean beans.
- The precise identities of these Se species in plants, including soybean, remain largely uncharacterized.
Purpose of the Study:
- To characterize Se-containing proteins in Se-enriched soybean beans using a multi-technique metallomics approach.
- To identify specific Se-bound peptides and proteins within soybean tissues.
Main Methods:
- Utilized two-dimensional high-performance liquid chromatography-inductively coupled plasma mass spectrometry (HPLC-ICP-MS).
- Employed size-exclusion chromatography (SEC) and anion-exchange chromatography (AEC) for protein separation.
- Applied HPLC-Chip-electrospray ion trap mass spectrometry (ESI-MS/MS) for peptide identification and mapping.
Main Results:
- Identified two main protein categories, maturation proteins and protease inhibitors, in Se-containing HPLC fractions.
- Discovered a Se-containing peptide, KSDQSSSYDDDEYSKPCCDLCMCTRS, belonging to the Bowman-Birk proteinase isoinhibitor from Glycine max.
- Developed and applied a novel method for Se-containing peptide identification based on non-specific incorporation.
Conclusions:
- Successfully characterized Se-containing proteins in Se-enriched soybean beans.
- Identified a specific Se-bound peptide linked to a known soybean proteinase inhibitor.
- Further research into the nutritional value of these Se-enriched proteins is warranted.
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