Characterization of D-myo-inositol 1,4,5-trisphosphate Phosphatase in Rat Brain

Overview

Journal Biochem Biophys Res Commun

Publisher Elsevier

Specialty Biochemistry

Date 1986 Jan 14

PMID 3004437

Citations 19

Authors

C Erneux

A Delvaux

C Moreau

J E Dumont

Affiliations

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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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