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Identification of a protein kinase activity in purified foot- and-mouth disease virus
1981
Journal of Virology
Purified preparations of foot-and-mouth disease virus types A, 0, and C contain a protein kinase activity which can transfer the gamma phosphate of [32P]ATP to virion structural proteins VP2 and VP3 and exogenous acceptor proteins. Utilizing protamine sulfate as an acceptor, the kinase activity can be demonstrated in disrupted virus but not in intact virus. The enzyme is heat labile with optimal activity at pH 7 or greater. Serine residues of protamine sulfate were identified as the amino acid
doi:10.1128/jvi.39.2.455-462.1981
fatcat:npyxieukhnf7bp7f7zfv3mbd2a