In situ activity-based protein profiling of serine hydrolases in E. coli
作者： Dmitry Shamshurin , Oleg V. Krokhin , David Levin , Richard Sparling , John A. Wilkins
DOI: 10.1016/J.EUPROT.2014.04.007
关键词:
摘要: A fluorophosphonate based alkyne activity probe was used for the selective labeling of active serine hydrolases in intact Escherichia coli cells. biotin-azide tag subsequently attached to functionality with copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction. Comparison proteins from in-cell and lysate labeled preparations suggested qualitatively similar patterns reactivity both preparations. Approximately 68%, 30 total 44 detectable E. were indicating significant coverage a single probe. The methods described here offer useful tool profiling monitoring hydrolase situ.
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