Premium
The effect of sodium tetradecyl sulfate on mobility and antigen detectability of microtubule proteins in sodium dodecyl sulfate‐polyacrylamide gel electrophoresis
Author(s) -
Hodgkinson Julie L.,
Steffen Walter
Publication year - 1997
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.1150181113
Subject(s) - sodium dodecyl sulfate , gel electrophoresis , chemistry , polyacrylamide gel electrophoresis , sodium , antigenicity , chromatography , biochemistry , biology , antigen , enzyme , genetics , organic chemistry
Several factors been reported to influence the mobility of polypeptide in sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) including the brand of SDS. Using microtubule proteins from axonemes of Lytechinus pictus and Spisula solidissima sperm and meiotic spindles of Spisula solidissima we demonstrate that the change in mobility was caused by sodium tetradecyl sulfate (STS), a major contaminant of many commercial SDS brands. We also examined the use of sodium tetradecyl sulfate and different SDS brands as a tool in extracting more information from immunoblot studies. Commercial SDS containing contaminants other than sodium tetradecyl sulfate reduced or eliminated the immunosignal from certain polypeptides and the loss of antigenicity could not even be recovered by immunoblot under “renaturing” conditions. It can thus be concluded that STS can be useful in separating and identifying comigrating polypeptides and in detecting additional immunobands in immunoblots.