Optimized Affinity Capture of Yeast Protein Complexes
Author(s) -
John LaCava,
Javier Fernández-Martı́nez,
Zhanna Hakhverdyan,
Michael P. Rout
Publication year - 2016
Publication title -
cold spring harbor protocols
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.674
H-Index - 51
eISSN - 1940-3402
pISSN - 1559-6095
DOI - 10.1101/pdb.prot087932
Subject(s) - elution , yeast , chromatography , chemistry , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , gel electrophoresis , affinity chromatography , solvent , protein purification , biochemistry , enzyme
Here, we describe an affinity isolation protocol. It uses cryomilled yeast cell powder for producing cell extracts and antibody-conjugated paramagnetic beads for affinity capture. Guidelines for determining the optimal extraction solvent composition are provided. Captured proteins are eluted in a denaturing solvent (sodium dodecyl sulfate polyacrylamide gel electrophoresis sample buffer) for gel-based proteomic analyses. Although the procedures can be modified to use other sources of cell extract and other forms of affinity media, to date we have consistently obtained the best results with the method presented.
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