PMID: 109431Jun 25, 1979

Purification and properties of prostaglandin D synthetase from rat brain.

The Journal of Biological Chemistry
T ShimizuO Hayaishi

Abstract

The prostaglandin D synthetase system was isolated from rat brain. Prostaglandin endoperoxide synthetase solubilized from a microsomal fraction catalyzed the conversion of arachidonic acid to prostaglandin H2 in the presence of heme and tryptophan. Prostaglandin D synthetase (prostaglandin endoperoxidase-D isomerase) catalyzing the isomerization of prostaglandin H2 to prostaglandin D2 was found predominantly in a cytosol fraction and was purified to apparent homogeneity with a specific activity of 1.7 mumol/min/mg of protein at 24 degrees C. The enzyme also acted upon prostaglandin G2 and produced a compound presumed to be 15-hydroperoxy-prostaglandin D2. Glutathione was not required for the enzyme reaction, but the enzyme was stabilized by thiol compounds including glutathione. The enzyme was inhibited by p-chloromercuribenzoic acid in a reversible manner. The purified enzyme was essentially free of the glutathione S-transferase activity which was found in the cytosol of brain.

Related Concepts

Metazoa
Brain
Chloromercuribenzoates
Kinetics
Microsomes
Molecular Weight
Prostaglandin-Endoperoxide Synthase
Prostaglandins D
Prostaglandins H
Serum Albumin, Bovine

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