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.
Bibliographical noteFunding Information:
Acknowledgements. This work was supported m part by grants from the Korea Science and Engineermg Foundation (KOSEF 89-07-02-04) and from Pohang University of Science and Technology. We would like to thank Dr. Sung Ki Jang for critical reading of the manuscript.
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
- Cell Biology