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 C 6 Bu-1 cells in the presence of GTPγS or Alp 4 − 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.
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