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. 2018 Mar 27;9(23):16489–16500. doi: 10.18632/oncotarget.24740

Figure 1. TpeLGTD glycosylates Ras proteins irrespective of nucleotide binding and hyperactive mutations in vitro.

Figure 1

(A) Relative initial glycosylation velocities were calculated from three independent experiments for K-Ras preloaded with GDP, GTP or GDP-AlF3. (B) Wild type as well as G12V mutated K-, H-, and N-Ras proteins were glycosylated by TpeLGTD. Shown are the autoradiogram (upper panel) and the Coomassie-stained gel (lower panel).