A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum

Do Sik Min, Yong Kim, Young Han Lee, Pann Ghill Suh, Sung Ho Ryu

Research output: Contribution to journalArticle

13 Citations (Scopus)

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 languageEnglish
Pages (from-to)38-42
Number of pages5
JournalFEBS Letters
Volume331
Issue number1-2
DOIs
Publication statusPublished - 1993 Sep 27

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Type C Phospholipases
Programmable logic controllers
GTP-Binding Proteins
Cerebellum
Isoenzymes
Membranes
Immune Sera
Chemical activation
Association reactions

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Min, Do Sik ; Kim, Yong ; Lee, Young Han ; Suh, Pann Ghill ; Ryu, Sung Ho. / A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-β4, from the particulate fraction of bovine cerebellum. In: FEBS Letters. 1993 ; Vol. 331, No. 1-2. pp. 38-42.
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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 journalArticle

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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

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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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