A G-PROTEIN-COUPLED 130-KDA PHOSPHOLIPASE-C ISOZYME, PLC-BETA-4, FROM THE PARTICULATE FRACTION OF BOVINE CEREBELLUM

Abstract

A 130 kDa PLC isozyme was purified from the particulate fraction of bovine cerebellum. This PLC was recognized by a polyclonal antiserum generated against the purified 97 kDa PLC-beta4. Reconstitution of the purified 130 kDa PLC with the membranes of C6 Bu-1 cells in the presence of GTPgammaS or AlF4- resulted in PLC activation as well as the association of PLC with the membranes. Both the association and activation were revoked when the membrane was washed with 2 M KCl. The 97 kDa PLC-beta4 did not associate with membranes. These data suggest that the 130 kDa PLC is the intact form of PLC-beta4 the activity of which is likely to be regulated by a G-protein on the membrane.