Chapter title |
Isolation of Native Soluble and Membrane-Bound Protein Complexes from Yeast Saccharomyces cerevisiae.
|
---|---|
Chapter number | 4 |
Book title |
Peroxisomes
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6937-1_4 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6935-7, 978-1-4939-6937-1
|
Authors |
Hansen, Tobias, Chan, Anna, Schröter, Thomas, Schwerter, Daniel, Girzalsky, Wolfgang, Erdmann, Ralf, Tobias Hansen, Anna Chan, Thomas Schröter, Daniel Schwerter, Wolfgang Girzalsky, Ralf Erdmann |
Editors |
Michael Schrader |
Abstract |
Immunoprecipitation is a traditional approach to isolate single proteins or native protein complexes from a complex sample mixture. The original method makes use of specific antibodies against endogenous proteins or epitope tags, which are first bound to the target protein and then isolated with protein A beads. An advancement of this method is the application of a protein A tag fused to the target protein and the affinity-purification of the tagged protein with human Immunoglobulin G chemically cross-linked to a sepharose matrix. This method will be described exemplified by the purification of protein complexes of the peroxisomal membrane from yeast Saccharomyces cerevisiae. |
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