Ma, Xiao and Wildgruber, Robert and Bauer, Johann and Weber, Gerhard and Infanger, Manfred and Grosse, Jirka and Grimm, Daniela (2012) The use of sigmoid pH gradients in free-flow isoelectric focusing of human endothelial cell proteins. ELECTROPHORESIS, 33 (9-10). pp. 1349-1355. ISSN 0173-0835,
Full text not available from this repository. (Request a copy)Abstract
Prefractionation of proteins enhances the resolution of proteome analysis of whole cells. Free-flow electrophoresis (FFE) provides a useful step in various prefractionation protocols, since matrix-free isoelectric focusing (FF-IEF) performed in this machine enables the enrichment of large, easily absorbable, sensitive proteins. The impact of the FFE on the success of a proteome analysis depends on the quality of the FF-IEF separation procedure. Therefore, attempts are continuously being made to improve FF-IEF. Here, we applied sigmoid pH gradients to the prefractionation of endothelial cell proteins. Small steps of pH incline between neighboring FFE fractions were established in pH ranges, in which the proteins of interest have their pIs. With the help of this advanced technology, we separated vimentin and cytoplasmic actin as well as triosephosphate isomerase and glyceraldehyde phosphate dehydrogenase preparatively, and found a pI of 5.9 +/- 0.2 for nonmuscle myosin.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | FIBROBLAST-GROWTH-FACTOR; THYROID-CARCINOMA CELLS; SIMULATED MICROGRAVITY; GEL-ELECTROPHORESIS; APOPTOSIS; WEIGHTLESSNESS; IDENTIFICATION; FRACTIONATION; DEHYDROGENASE; PURIFICATION; Cytoskeletal proteins; Glycolytic enzymes; Isoelectric point; Phosphoglycerate kinase; Polypeptide chain cleavage |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Abteilung für Nuklearmedizin |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 May 2020 06:35 |
| Last Modified: | 14 May 2020 06:35 |
| URI: | https://pred.uni-regensburg.de/id/eprint/18780 |
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