In vitro palmitoylation of native bovine brain G_oα

The native G_oα was purified from bovine brain cortex and palmitoylated in vitro. The in vitro palmitoylation site was the same as that in vivo. The internal palmitoylation of purified native G_oα was found to be largely maintained. The apparant palmitoylation ratio was significantly increased after the G_oα was treated with DTT. The GTPγS binding characteristic of G_oα was not influenced by palmitoylation, however, the affinity for LUVs was increased dramatically. The in vitro palmitoylation model of G_oα provides a better basis for studying the functional role of G protein palmitoylation in signal transduction.