Human cytomegalovirus virion-associated protein with kinase activity

WJ Britt, D Auger - Journal of virology, 1986 - Am Soc Microbiol
WJ Britt, D Auger
Journal of virology, 1986Am Soc Microbiol
Protein kinase activity was detected in immunoprecipitates of human cytomegalovirus
virions and infected cells by using a monoclonal antibody directed against an abundant
68,000-dalton virion structural protein. Purification of this protein by electrophoresis
confirmed that the kinase activity was associated with this protein. The kinase activity was
dependent on divalent cations (Mg2+, Mn2+) and cyclic nucleotide independent and
exhibited optimal activity at pH 7 to 8. The kinase phosphorylated threonine and serine but …
Protein kinase activity was detected in immunoprecipitates of human cytomegalovirus virions and infected cells by using a monoclonal antibody directed against an abundant 68,000-dalton virion structural protein. Purification of this protein by electrophoresis confirmed that the kinase activity was associated with this protein. The kinase activity was dependent on divalent cations (Mg2+, Mn2+) and cyclic nucleotide independent and exhibited optimal activity at pH 7 to 8. The kinase phosphorylated threonine and serine but not tyrosine.
American Society for Microbiology