title: Phosphorylated protein component present in influenza virions.
abstract: The nucleoprotein of the WSN strain of influenza was found to be phosphorylated in vitro. 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.
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism; D006851:Hydrochloric Acid; D006868:Hydrolysis; D009975:Orthomyxoviridae / Q000032:analysis*; D010750:Phosphoproteins / Q000032:analysis*; D012367:RNA, Viral / Q000032:analysis; D012694:Serine / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis*
chemical_list: D010750:Phosphoproteins; D012367:RNA, Viral; D014764:Viral Proteins; D012694:Serine; D000469:Alkaline Phosphatase; D006851:Hydrochloric Acid