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.
| Original language | English |
|---|---|
| Pages (from-to) | 38-42 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 331 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - 1993 Sep 27 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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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