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J. Biol. Chem., Vol. 260, Issue 23, 12410-12415, 10, 1985
Y Urade, N Fujimoto and O Hayaishi
Prostaglandin D synthetase was purified 2,600-fold from rat brain to
apparent homogeneity, as judged by polyacrylamide gel electrophoresis and
ultracentrifugation. The purified enzyme was a monomeric protein with a
molecular weight of 27,000 +/- 1,000. The pI value, sedimentation
coefficient, and partial specific volume were 4.6, 4.1 s, and 0.73 ml/g,
respectively. The enzyme was stable between pH 4 and 11 at the temperature
lower than 25 degrees C and resistant to a heat treatment under alkaline
conditions (pH 8-11). About 50% of the activity was detected after a heat
treatment at 100 degrees C for 5 min at pH 10. However, the enzyme was
readily inactivated by the isomerase reaction of prostaglandin H2 to
prostaglandin D2. The enzyme required sulfhydryl compounds such as
dithiothreitol, glutathione, beta- mercaptoethanol, cysteine, and
cysteamine for the reaction, but stoichiometric oxidation of these
sulfhydryl compounds was not observed. The optimum pH, Km value for
prostaglandin H2, and the turnover number were 9.5, 14 microM, and 170
min-1, respectively. The antibody was raised against the purified enzyme in
a rabbit, which showed only one positive band in immunoblotting after gel
electrophoresis of crude extracts of the brain at the same position as that
of the purified enzyme. More than 90% of the prostaglandin D synthetase
activity in the brain was absorbed by an excess amount of the antibody,
indicating that our preparation is a major component of the enzyme
responsible for the biosynthesis of prostaglandin D2 in the brain.
Purification and characterization of rat brain prostaglandin D synthetase
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