| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7596778 | Food Chemistry | 2014 | 5 Pages |
Abstract
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 β-d-maltoside detergent in the solubilisation buffer combined with the IEF approach. Several well focalized protein spots were obtained and analyzed through mass-spectrometry.
Related Topics
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Chemistry
Analytical Chemistry
Authors
Federica Mainente, Gianni Zoccatelli, Marilinda Lorenzini, Daniela Cecconi, Simone Vincenzi, Corrado Rizzi, Barbara Simonato,