Abstract
The potential of electron capture dissociation (ECD) was translated into identification of heavily-modified proteins from eukaryotic proteins isolated from S. cerevisiae. Yeast cells were grown to stationary phase and collected by centrifugation. Cell lysis by sonication was followed by fractionation of the cell extract using a combination of continuous-elution PAGE and reversed-phase HPLC. It was found that ∼40-50% of fragment ions from standard threshold dissociation techniques do not occur in strings, for ions of ∼75 wild-type proteins.
Original language | English (US) |
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Title of host publication | Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics |
Pages | 101-102 |
Number of pages | 2 |
State | Published - 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