AI Article Synopsis
- Native polyacrylamide electrophoresis was used with two reversible anionic stains, Ponceau S and Ponceau 2R, to investigate the oligomeric states of soluble proteins.
- The stains caused a charge shift in nondissociated protein oligomers, allowing for their separation based on size under physiological conditions.
- After electrophoresis, the stains could be washed away, and protein complexes were visualized through enzyme activity or a nonspecific protein stain, highlighting enzyme activities like glycosidases, lactate dehydrogenase, and phosphatases.
Article Abstract
Native polyacrylamide electrophoresis in the presence of two reversible protein anionic stains (Ponceau S and Ponceau 2R) was used to study the oligomeric states of soluble proteins. A mild binding of the used protein stains to nondissociated protein oligomers imposed a charge shift on the proteins resulting into separation of protein species according to their size under physiological conditions. Adsorbed stains could be easily removed after electrophoresis by washing of polyacrylamide gel with buffer and protein complexes could be visualized either by the detection of their enzyme activity or by using a nonspecific protein stain. The specific detection of enzyme activity of glycosidases, lactate dehydrogenase, or phosphatases was shown as an example.
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| http://dx.doi.org/10.1002/jssc.201000869 | DOI Listing |
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