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Suh, Pann-Ghill
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A G-PROTEIN-COUPLED 130-KDA PHOSPHOLIPASE-C ISOZYME, PLC-BETA-4, FROM THE PARTICULATE FRACTION OF BOVINE CEREBELLUM

Author(s)
Min, Do SikKim, YongLee, Young HanSuh, Pann-GhillRyu, Sung Ho
Issued Date
1993-09
DOI
10.1016/0014-5793(93)80293-4
URI
https://scholarworks.unist.ac.kr/handle/201301/16498
Fulltext
http://www.sciencedirect.com/science/article/pii/0014579393802934
Citation
FEBS LETTERS, v.331, no.1-2, pp.38 - 42
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-beta4. Reconstitution of the purified 130 kDa PLC with the membranes of C6 Bu-1 cells in the presence of GTPgammaS or AlF4- 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 KCl. The 97 kDa PLC-beta4 did not associate with membranes. These data suggest that the 130 kDa PLC is the intact form of PLC-beta4 the activity of which is likely to be regulated by a G-protein on the membrane
Publisher
ELSEVIER SCIENCE BV
ISSN
0014-5793

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