Characterization of D-myo-inositol 1,4,5-trisphosphate phosphatase in rat brain.


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.

Cite this paper

@article{Erneux1986CharacterizationOD, title={Characterization of D-myo-inositol 1,4,5-trisphosphate phosphatase in rat brain.}, author={Christophe Erneux and Anne Delvaux and Colette Moreau and Jacques E. Dumont}, journal={Biochemical and biophysical research communications}, year={1986}, volume={134 1}, pages={351-8} }