Phosphorylated protein component present in influenza virions

M. L. Privalsky, E. E. Penhoet

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

The nucleoprotein of the WSN strain of influenza was found to be phosphorylated in vivo. The phosphate-protein bond was stable to hot trichloroacetic acid, RNase, DNase, succinic acid, and succinic acid-hydroxylamine, but sensitive to hydrolysis by bacterial alkaline phosphatase. This suggested that the nucleoprotein is in the form of a phosphomonoester. Acid hydrolysis of the isolated nucleoprotein followed by thin-layer electrophoresis identified the phosphorylated amino acid residue as phosphoserine.

Original languageEnglish (US)
Pages (from-to)401-405
Number of pages5
JournalJournal of Virology
Volume24
Issue number1
StatePublished - 1977

ASJC Scopus subject areas

  • Immunology

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