Anomalous electrophoretic behavior of the major potato virus X RNA translation product.

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 Methods

authors

Karasev AV,Miroshnichenko NA,Rozanov MN

doi

10.1016/0166-0934(89)90136-5

subject

Has Abstract

pub_date

1989-02-01 00:00:00

pages

223-7

issue

2

eissn

0166-0934

issn

1879-0984

pii

0166-0934(89)90136-5

journal_volume

23

pub_type

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