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. Author manuscript; available in PMC: 2009 Oct 25.
Published in final edited form as: Virology. 2008 Aug 30;380(2):276–284. doi: 10.1016/j.virol.2008.07.013

Fig. 8. SAH binding of YFV methyltransferases.

Fig. 8

SAH was covalently bound via the free amino group of the homocysteine moiety to Sepharose using an N-hydroxysuccinimidyl linkage. Purified 6X His tagged methyltransferases (amino acid number G1 to D296) of YFV wild type (WT), S56A, S56D and CFP were incubated overnight with SAH bound to Sepharose and after being washed with 50 column volumes of PBS+0.5% NP40, bound protein was eluted, spotted on a PVDF membrane via a dot blot apparatus and the amount of bound protein was measured by western blot with anti-His antibody.