Different properties of the native and reconstituted heterotrimeric G protein transducin

A novel method is described for G protein transducin (Gt) purification from native bovine rod photoreceptor membranes without subunit dissociation caused by exposure to photoactivated rhodopsin (Rho*). The results shed light on differences in conformation and heterotrimer complex formation between the two preparations or altered stability of the reconstituted Gt that assembles differently than the native protein.