Phosphorylated protein component present in influenza virions.
AUTOR(ES)
Privalsky, M L
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=515941Documentos Relacionados
- Selective dansylation of M protein within intact influenza virions.
- Structural components of influenza C virions.
- pIRS1 and pTRS1 are present in human cytomegalovirus virions.
- Influenza A virus M2 protein: monoclonal antibody restriction of virus growth and detection of M2 in virions.
- Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions.
