High Throughput Identification, Purification and Structural Characterization of Water Soluble Protein Complexes in Desulfovibrio vulgaris [electronic resource].
- Berkeley, Calif. : Lawrence Berkeley National Laboratory, 2010.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy.
- Physical Description:
- 1 : digital, PDF file
- Additional Creators:
- Lawrence Berkeley National Laboratory
United States. Department of Energy. Office of Scientific and Technical Information
- Our scheme for the tagless purification of water soluble complexes. 10 g of protein from a crude bacterial extract is first fractionated by ammonium sulfate precipitation and then by a series of chromatographic steps: anion exchange (IEX), hydrophobic interaction (HIC), and finally size exclusion (Gel Filtration). Fractions from the last chromatography step are trypsin digested and peptides labeled with iTRAQ reagents to allow multiplexing and quantitation during mass spectrometric analysis. Elution profiles of identified proteins are then subjected to clustering analysis.
- Published through SciTech Connect.
110th General Meeting of the American Society for Microbiology, San Diego, CA, May 23-27, 2010.
Hazen, Terry; Yang, Li; Liu, Hui-Hai; Choi, M.; Dong,, Ming; Han, Bong-Gyoon; Malik, J.; Geller, Jil; Chandonia, John-Marc; Arbelaez, Pablo; Sterling, H. J.; Typke, Dieter; Shatsky, Max; Brenner, Steve; Fisher, Susan; Williams, Evan; Szakal, Evelin; Allen, S.; Hall, S. C.; Witkowska, H. E.; Jin, Jiming; Glaeser, Robert; Biggin, Mark.
Earth Sciences Division
Life Sciences Division
- Funding Information:
View MARC record | catkey: 14129670