A highly efficient approach for proteomic study of protein complexes

Georgia Dolios, Dora Dias, Zhen Qiang Pan, Rong Wang

Research output: Contribution to conferencePaperpeer-review

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 languageEnglish
Pages449-450
Number of pages2
StatePublished - 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: 2 Jun 20026 Jun 2002

Conference

ConferenceProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/TerritoryUnited States
CityOrlando, FL
Period2/06/026/06/02

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