Simultaneous determination of native and subunit molecular weights of proteins by pore limit electrophoresis and restricted use of sodium dodecyl sulfate

Abstract

In the present communication, we describe a method for the determination of both the native and subunit molecular weight of a protein by a single pore limit electrophoretic run. When native proteins and sodium dodecyl sulfate (SDS)-heat denatured proteins were electrophoresed in a 4-28% gradient-polyacrylamide gel, in the presence of 0.02% SDS in running buffer, their respective molecular weights (native and subunit) could be determined by comparing the migration distances of unknown and standard proteins. The presence of SDS up to 0.02% in the running buffer did not dissociate the native proteins into their subunits. The linearity in distribution of native and SDS-polyacrylamide gel electrophoresis (PAGE) standard marker proteins used for the molecular weight determination further showed the efficacy of the present technique.