In vitro palmitoylation of native bovine brain G(o)alpha

The native G(o)alpha was purified from bovine brain cortex and palmitoylate d in vitro. The in vitro palmitoylation site was the same as that in vivo. The internal palmitoylation of purified native G(o)alpha was found to be la rgely maintained. The apparant palmitoylation ratio was significantly incre ased after the G(o)alpha was treated with DTT The GTP gammaS binding charac teristic of G(o)alpha was not influenced by palmitoylation, however, the af finity for LUVs was increased dramatically. The in vitro palmitoylation mod el of G(o)alpha provides a better basis for studying the functional role of G protein palmitoylation in signal transduction.