Anomalous electrophoretic behavior of the major potato virus X RNA translation product.
The major potato virus X (PVS) RNA translation product migrates in Laemmli's electrophoresis system as a 210 kDa polypeptide ('p210'). If a Tris-phosphate-SDS buffer system is used instead of a Tris-glycine-SDS one, the mobility of p210 is higher than that of the largest TMV RNA translation product, the 183 kDa protein. It is suggested that anomalous electrophoretic behavior of the largest PVX polypeptide during SDS-electrophoresis is due to its primary structure, namely to the presence of hydrophilic domains.
Karasev
A V
AV
Institute of Microbiology, Academy of Sciences of the USSR, Moscow.
Miroshnichenko
N A
NA
Rozanov
M N
MN
D002499:Centrifugation, Density Gradient; D004591:Electrophoresis, Polyacrylamide Gel; D010942:Plant Viruses / Q000235:genetics*; D014176:Protein Biosynthesis; D012367:RNA, Viral / Q000235:genetics*; D011198:Solanum tuberosum; D014764:Viral Proteins / Q000032:analysis* / Q000235:genetics
D012367:RNA, Viral; D014764:Viral Proteins