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 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum. / Min, Do Sik; Kim, Yong; Lee, Young Han; Suh, Pann Ghill; Ryu, Sung Ho.
In: FEBS Letters, Vol. 331, No. 1-2, 27.09.1993, p. 38-42.Research output: Contribution to journal › Article
TY - JOUR
T1 - A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum
AU - Min, Do Sik
AU - Kim, Yong
AU - Lee, Young Han
AU - Suh, Pann Ghill
AU - Ryu, Sung Ho
PY - 1993/9/27
Y1 - 1993/9/27
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0027362142&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(93)80293-4
DO - 10.1016/0014-5793(93)80293-4
M3 - Article
C2 - 8405407
AN - SCOPUS:0027362142
VL - 331
SP - 38
EP - 42
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-2
ER -