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Preliminary studies on selenium-containing proteins in Brassica juncea by size exclusion chromatography and fast protein liquid chromatography coupled to ICP-MS

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DOIResolve DOI: https://doi.org/10.1039/b312960h
AuthorSearch for: ; Search for: ORCID identifier: https://orcid.org/0000-0002-3349-5535; Search for:
FormatText, Article
Abstract
An approach for screening and resolving selenium-containing plant proteins was developed based on the combination of sample preparation and multi-dimensional liquid chromatography coupled to ICP-MS. Different protein extraction protocols were investigated. A 24 h dodecylsulfate-mediated protein extraction in a sonication bath followed by acetone precipitation was found to be optimal. The use of different protein precipitate solubilizing agents (sodium dodecyl sulfate media and Tris-HCl buffer) demonstrates possible fractionation of the selenium-containing proteins. Selenium-containing protein screening and fractionation were carried out by means of SEC-ICP-MS. High molecular weight selenium containing proteins were solubilized with a sodium dodecyl sulfate-containing buffer, whereas the low molecular weight compounds were released into a Tris-HCl buffer. Size exclusion chromatography–fast protein liquid chromatography coupled to ICP-MS allowed separation and detection of several selenium-containing proteins in Se-supplemented wild type Brassica juncea plant, a fast growing selenium accumulator.
Publication date
PublisherRoyal Society of Chemistry
In
  • The Analyst 129, no. 2: 116–.
LanguageEnglish
Peer reviewedYes
NRC publication
This is a non-NRC publication

"Non-NRC publications" are publications authored by NRC employees prior to their employment by NRC.

NPARC number23001833
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Record identifier6b63c8fe-3a27-40d1-bc6b-721c21b5ce98
Record created2017-04-18
Record modified2020-04-17
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