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SDS disc electrophoresis of proteins in homogeneous, low‐concentrated polyacrylamide gels
Author(s) -
Maly I. Piotr,
Nitsch Cordula
Publication year - 2007
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.200600688
Subject(s) - acrylamide , stacking , chromatography , polyacrylamide gel electrophoresis , chemistry , tris , polyacrylamide , electrophoresis , buffer (optical fiber) , counterion , capillary electrophoresis , ion , polymer chemistry , biochemistry , organic chemistry , polymer , telecommunications , computer science , copolymer , enzyme
In the attempt to separate in a single gel run low‐ and high‐molecular‐weight proteins, we present here a multiphasic buffer system designed for this purpose. It avoids the continuous stacking of SDS as it occurs in the ’classical' SDS‐PAGE. The system allows complete stacking and destacking of proteins in the 3.5–250 kDa range at acrylamide concentrations as low as 4.5% T (total acrylamide concentration in %) and 2.6% C (degree of cross‐linking in %). Taurine is used as the trailing ion in the cathode buffer and in the resolving zone of the gel, and two different counterions (Tris and imidazole) in the stacking zone. The gel system is easy to prepare and, due to the very low acrylamide concentrations, it is ideal for analytical as well as for preparative tasks.