Abstract
The development of general methods for identifying and characterizing intact proteins in high throughput manner, using native proteins from Methanococcus jannaschii, was discussed. A 2-D separation to sufficiently fractionate the soluble portion of the proteome, followed by automated fourier transform mass spectrometry (FTMS) and MS/MS for the proteins in these samples, with a modified THRASH algorithm were used to analyze the data. The soluble portion of the lysate was separated via preparative denatured polyacrylamide gel electrophoresis. The protein precipitation had demonstrated high recovery, and the resolution of the HPLC traces indicated that the acid-labile surfactant (ALS) was both removed or degraded by the precipitation steps.
Original language | English (US) |
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Title of host publication | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
Pages | 239-240 |
Number of pages | 2 |
State | Published - Dec 1 2002 |
Event | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002 |
Other
Other | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
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Country/Territory | United States |
City | Orlando, FL |
Period | 6/2/02 → 6/6/02 |
ASJC Scopus subject areas
- Spectroscopy