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In agreement with this, the tobacco leaf nuclear extract retarded the electrophoretic mobility of each of the eight oligonucleotides.
Proteins were separated by sodium dodecyl sulphate/polyacrylamide gel electrophoresis as described previously.
After electrophoresis, the proteins were transferred electrophoretically onto a nitrocellulose membrane as described previously.
The most common approach to these ends is the determination of the electrophoretic mobility of lipid vesicles in electrolyte solutions.
One can study membrane protein formation and aggregation by examining the electrophoretic mobility of dimerizing proteins subject to point mutations.
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