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 |
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Pages | 101-102 |
Number of pages | 2 |
State | Published - 2002 |
Externally published | Yes |
Event | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: 2 Jun 2002 → 6 Jun 2002 |
Conference
Conference | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
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Country/Territory | United States |
City | Orlando, FL |
Period | 2/06/02 → 6/06/02 |