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. © 1993.
Min, D. S., Kim, Y., Lee, Y. H., Suh, P. G., & Ryu, S. H. (1993). A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum. FEBS Letters, 331(1–2), 38–42. https://doi.org/10.1016/0014-5793(93)80293-4