SIMULTANEOUS DETERMINATION OF NATIVE AND SUBUNIT MOLECULAR-WEIGHTS OFPROTEINS BY PORE LIMIT ELECTROPHORESIS AND RESTRICTED USE OF SODIUM DODECYL-SULFATE
Rk. Tyagi et al., SIMULTANEOUS DETERMINATION OF NATIVE AND SUBUNIT MOLECULAR-WEIGHTS OFPROTEINS BY PORE LIMIT ELECTROPHORESIS AND RESTRICTED USE OF SODIUM DODECYL-SULFATE, Electrophoresis, 14(8), 1993, pp. 826-828
In the present communication, we describe a method for the determinati
on of both the native and subunit molecular weight of a protein by a s
ingle 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 r
unning buffer, their respective molecular weights (native and subunit)
could be determined by comparing the migration distances of unknown a
nd standard proteins. The presence of SDS up to 0.02% in the running b
uffer did not dissociate the native proteins into their subunits. The
linearity in distribution of native and SDS-polyacrylamide gel electro
phoresis (PAGE) standard marker proteins used for the molecular weight
determination further showed the efficacy of the present technique.