Phosphorylated protein component present in influenza virions

Abstract
The nucleoprotein of the WSN strain of influenza was 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 [Escherichia coli] alkaline phosphatase. 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.