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Buffers to suppress sodium dodecyl sulfate adsorption to polyethylene oxide for protein separation on capillary polymer electrophoresis
Author(s) -
Sumitomo Keiko,
Mayumi Koichi,
Minamikawa Hiroyuki,
Masuda Mitsutoshi,
Asahi Toru,
Shimizu Toshimi,
Ito Kohzo,
Yamaguchi Yoshinori
Publication year - 2011
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201000497
Subject(s) - tris , sodium dodecyl sulfate , capillary electrophoresis , adsorption , polymer , chromatography , electrophoresis , chemistry , dynamic light scattering , chemical engineering , organic chemistry , nanoparticle , biochemistry , engineering
Although polyethylene oxide (PEO) offers several advantages as a sieving polymer in SDS capillary polymer electrophoresis (SDS‐CPE), solution properties of PEO cause deterioration in the electrophoresis because PEO in solution aggregates itself, degrades into smaller pieces, and forms polymer–micelle complexes with SDS. We examined protein separation on SDS‐CPE with PEO as a sieving matrix in four individual buffer solutions: Tris‐CHES, Tris‐Gly, Tris‐Tricine, and Tris‐HCl buffers. The solution properties of PEO as a sieving matrix in those buffers were examined by dynamic light scattering (DLS) and by surface tension. Preferential SDS adsorption onto PEO disturbed protein–SDS complexation and impaired the protein separation efficiency. Substantial adsorption of SDS to PEO was particularly observed in Tris‐Gly buffer. The Tris‐CHES buffer prevented SDS from adsorbing onto the PEO. Only Tris‐CHES buffer achieved separation of six proteins. This study demonstrated efficient protein separation on SDS‐CPE with PEO.