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  • Title: Characterization of D-myo-inositol 1,4,5-trisphosphate phosphatase in rat brain.
    Author: Erneux C, Delvaux A, Moreau C, Dumont JE.
    Journal: Biochem Biophys Res Commun; 1986 Jan 14; 134(1):351-8. PubMed ID: 3004437.
    Abstract:
    Rat brain homogenates contain significant amounts of inositol 1,4,5-trisphosphate phosphatase in both 180,000xg (60 min) particulate and supernatant fractions. As other membrane-bound enzymes (e.g. guanylate cyclase), particulate inositol 1,4,5-trisphosphate phosphatase activity is highly sensitive to low concentrations of Triton X-100 (0.03%). Higher concentrations of detergent (1%) partially solubilized the enzyme. Thiol blocking agents (e.g. p-hydroxymercuribenzoate) inactivate inositol 1,4,5-trisphosphate phosphatase activity (an effect reversed with 2-mercaptoethanol). It is thus suggested that enzymatic activity requires the presence of -SH groups.
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