Resolution of simian virus 40 proteins in whole cell extracts by two-dimensional electrophoresis: heterogeneity of the major capsid protein.

摘要: Abstract The major capsid protein (VP1) of simian virus 40 (SV40) has been analyzed by two-dimensional electrophoresis. This system separates according to isoelectric point isoelectric-focusing, and molecular weight sodium dodecylsulphate electrophoresis (O'Farrell 1975). VP1 synthesis in infected CV-1 cells can be monitored directly analysis unfractionated whole cell extracts; the resolution from cellular proteins allows its detection as early 13 hr after infection. separation reveals that it is heterogeneous, consisting one (molecular 47,000 daltons approximately pH 6.8) five minor components. forms are 10% total differ form both (by 500 daltons) (ranging 6.7 6.9). Evidence presented show two phosphorylated derivatives VP1, further suggested all different result modifications primary product translation. A temperature-sensitive mutant BC complementation group (BC11) SV40 results with an altered electrophoretic mobility; shifted their points. In addition specific case SV40, aspects these studies should generally significant investigators studying eucaryotic gene expression gel electrophoresis: first, genetic origin a determined mutation which causes charge change resultant protein; second, or more spots on may products single gene.