A metabolite of halothane covalently binds to an endoplasmic reticulum protein that is highly homologous to phosphatidylinositol-specific phospholipase C-α but has no activity

Jackie L. Martin, Neil R. Pumford, Angela C. LaRosa, Brian M. Martin, Heloisa M.S. Gonzaga, Michael A. Beaven, Lance R. Pohl

Research output: Contribution to journalArticle


When the inhalation anesthetic halothane was administered to rats, a 58 kDa protein in the liver became covalently labeled by the trifluoroacetyl chloride metabolite of halothane. The amino acid sequences of the N-terminal and of several internal peptide fragments of the protein were 99% homologous to that of the deduced amino acid sequence of a cDNA reported to correspond to phosphatidylinositol-specific phospholipase C-α. The purified trifluoroacetylated 58 kDa protein or native 58 kDa protein, however, did not have phosphatidylinositol-specific phospholipase C activity. We conclude that the reported cDNA of phosphatidylinositol-specific phospholipase C-α may encode for a microsomal protein of unknown function.

Original languageEnglish (US)
Pages (from-to)679-685
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Jul 31 1991


ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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