Structural and enzymatic characterization of viper C-type virus

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Abstract
Summary The structural polypeptides of purified viper virus range in molecular weight from 11,000 to 97,000 daltons and consist of 3 major and about 13 minor polypeptides. The virus contains both protein kinase and reverse transcriptase activities. Several of the structural polypeptides are phosphorylatedin vitro by the virus-associated protein kinase. However, most (possibly all) of the viral structural polypeptides are not phosphorylatedin vivo. DeoxyATP is as efficient as ATP in donating phosphate forin vitro phosphorylation of viral proteins.In vitro protein phosphorylation always precedes transcription and the virus-associated protein kinase and reverse transcriptase activities can be partially separated by sedimentation in a sucrose gradient.