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. 1987 May;61(5):1708–1711. doi: 10.1128/jvi.61.5.1708-1711.1987

Polyomavirus major capsid protein VP1 is modified by tyrosine sulfuration.

J W Ludlow, R A Consigli
PMCID: PMC254161  PMID: 3033299

Abstract

Polyomavirus was propagated in primary mouse kidney cell monolayers and 35S-sulfate labeled by maintaining the infected cells in serum-free Eagle medium supplemented with 35S-labeled sodium sulfate. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of CsCI gradient-purified 35S-sulfate-labeled virions followed by fluorography indicated that the polyomavirus-coded major capsid protein VP1 incorporated this radiolabel. Two-dimensional gel electrophoresis followed by fluorography revealed 35S-sulfate incorporation into only two of the six VP1 isoelectric species (E and F). Amino acid analysis of 35S-sulfate labeled VP1 by enzymatic hydrolysis followed by two-dimensional thin-layer electrophoresis revealed the presence of 35S-sulfate-labeled tyrosine-O-sulfate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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