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

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