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Biomolecular Research Institute Ltd, 343 Royal Parade, Parkville, Victoria 3052, Australia
The hepatitis B virus X-protein (HBx) has been expressed in Escherichia coli both as an unfused protein and with an N-terminal hexaHis-containing fusion sequence. Both forms of HBx, after purification, displayed a potent AMP kinase activity, in which HBx phosphorylates AMP to ADP, using ATP as the exclusive phosphate donor. We also found that HBx has previously unreported GTPase and GTP-ADP nucleoside diphosphate kinase activities.
* Author for correspondence. Fax +61 3 342 4301. e-mail Theod@mel.dbe.csiro.au
Received 9 July 1995;
accepted 15 August 1995.
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