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Multifunctional Reagents for Quantitative Proteome‐Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development
Author(s) -
Broncel Malgorzata,
Serwa Remigiusz A.,
Ciepla Paulina,
Krause Eberhard,
Dallman Margaret J.,
Magee Anthony I.,
Tate Edward W.
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201500342
Subject(s) - lipid anchored protein , proteome , chemistry , myristoylation , reagent , proteomics , biochemistry , human proteome project , biology , membrane , apoptosis , autophagy , gene
Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direct detection of lipid‐modified tryptic peptides by mass spectrometry. This method enables high‐confidence identification of the myristoylated proteome on an unprecedented scale in cell culture, and allowed the first quantitative analysis of dynamic changes in protein lipidation during vertebrate embryonic development.