A highly efficient approach for proteomic study of protein complexes

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

A highly efficient approach for proteomic study of protein complexes

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

Research output: Contribution to conference › Paper › peer-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 language	English
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
Country/Territory	United States
City	Orlando, FL
Period	2/06/02 → 6/06/02

Cite this

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title = "A highly efficient approach for proteomic study of protein complexes",

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.",

author = "Georgia Dolios and Dora Dias and Pan, {Zhen Qiang} and Rong Wang",

year = "2002",

language = "English",

pages = "449--450",

note = "Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics ; Conference date: 02-06-2002 Through 06-06-2002",

}

TY - CONF

T1 - A highly efficient approach for proteomic study of protein complexes

AU - Dolios, Georgia

AU - Dias, Dora

AU - Pan, Zhen Qiang

AU - Wang, Rong

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=2442656891&partnerID=8YFLogxK

M3 - Paper

AN - SCOPUS:2442656891

SP - 449

EP - 450

T2 - Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics

Y2 - 2 June 2002 through 6 June 2002

ER -

A highly efficient approach for proteomic study of protein complexes

Abstract

Conference

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