Abstract:
: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.
journal_name
J Virol Methodsjournal_title
Journal of virological methodsauthors
Karasev AV,Miroshnichenko NA,Rozanov MNdoi
10.1016/0166-0934(89)90136-5subject
Has Abstractpub_date
1989-02-01 00:00:00pages
223-7issue
2eissn
0166-0934issn
1879-0984pii
0166-0934(89)90136-5journal_volume
23pub_type
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journal_title:Journal of virological methods
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