1887

Abstract

Summary

Preparations of the 30 × 10 mol. wt. protein (p30) of Rauscher murine leukaemia virus (R-MuLV) which had been purified to homogeneity as judged by gel electrophoresis in the presence of SDS and by amino-terminal amino acid analysis, showed considerable isoelectric heterogeneity. It was found that R-MuLV p30 polypeptide chains are easily converted into chains with more acidic isoelectric points. R-MuLV p30 polypeptides with different isoelectric points displayed the same set of I-labelled tryptic peptides. It is concluded that the charge heterogeneity of R-MuLV p30, as revealed in isoelectric focusing experiments, is not caused by genetic heterogeneity of the virus genome but by post-translational modification.

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/content/journal/jgv/10.1099/0022-1317-51-2-409
1980-12-01
2019-11-19
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-51-2-409
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