Abstract
The identification of the multiple components of the ROC1-cullin-based ubiquitin E3 ligase protein complex was discussed. The tryptic peptides obtained from the immunoprecipitation of Flag-ROC1 proteins were analyzed by micro-HPLZ/electropray ionization ion trap mass spectrometry (μHPLC/ESI-IT-MS) using data independent function. It was observed that low levels of signalosome/proteasome were detected in the Flag-ROC1 immunoprecipitates, which showed that the linkage between signalosome/proteasome and ROC1-cullin complexes was mediated by low affinity interactions. It was also observed that the use of ionic exchange column-based chromatography subsequent to affinity purification separated multiple ROC1-associatd protein species.
Original language | English |
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Pages | 449-450 |
Number of pages | 2 |
State | Published - 2002 |
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 |