Red wine proteins: two dimensional (2-D) electrophoresis and mass spectrometry analysis.
Food Chem
; 164: 413-7, 2014 Dec 01.
Article
in En
| MEDLINE
| ID: mdl-24996352
ABSTRACT
The aim of the present study was to optimize protein extraction from red wine (cv. Cabernet) in order to obtain a separation by two-dimensional electrophoresis (2-DE) compatible with mass spectrometry identification. Proteins were denatured by sodium dodecyl-sulphate (SDS) and precipitated as potassium salts. The potassium-DS (KDS) protein complexes obtained were treated with different solutions in order to remove the detergent. Proteins were solubilized with different buffers and separated by different electrophoretic approaches [native, urea, acid urea PAGEs and isoelectric focusing (IEF)] as the first-dimension (1-DE). The best 2D separation was achieved by using 10% saccharose in the DS removal step, and 6-cyclohexylhexyl ß-d-maltoside detergent in the solubilisation buffer combined with the IEF approach. Several well focalized protein spots were obtained and analyzed through mass-spectrometry.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Plant Proteins
/
Wine
/
Vitis
Type of study:
Prognostic_studies
Language:
En
Journal:
Food Chem
Year:
2014
Document type:
Article
Affiliation country: