Efficient extraction of nucleolar proteins for interactome analyses
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Updated: Jun 12, 2026

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling
Published on: November 17, 2019
Delphine Chamousset1, Sarah Mamane, François-Michel Boisvert
1Department of Cellular & Molecular Medicine, University of Ottawa, Ottawa, ON, Canada.
Abstract:
The efficient extraction of proteins from purified cellular organelles is critical for in vitro analyses, including identification of protein complex members by affinity purification-based quantitative proteomic approaches. When applied to purified nucleoli, classic nuclear protein extraction methods inefficiently and selectively release only approximately 50% of proteins. Here, we present a method that can extract up to 90% of nucleolar proteins, and apply it in a quantitative interactomic approach to identify nucleolar interaction partners for a mammalian protein phosphatase.
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