A G‐protein‐coupled 130 kDa phospholipase C isozyme, PLC‐β4, from the particulate fraction of bovine cerebellum

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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‐β4. Reconstitution of the purified 130 kDa PLC with the membranes of C6 Bu‐1 cells in the presence of GTPγS or Alp4 − 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 KC1. The 97 kDa PLC‐β4 did not associate with membranes. These data suggest that the 130 kDa PLC is the intact form of PLC‐β4 the activity of which is likely to be regulated by a G‐protein on the membrane.