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  • Title: PGD2 formation in the vasculature: characteristics of rat tail vein prostaglandin endoperoxide-D isomerase.
    Author: Gerritsen ME.
    Journal: Prostaglandins; 1983 Jan; 25(1):105-20. PubMed ID: 6573722.
    Abstract:
    Rat tail vein homogenates, microsome and high speed supernatant fractions were incubated with [1-(14) C]prostaglandin endoperoxide (PGH2) and products separated and identified by radio-thinlayer chromatography. PGI2 synthase was localized to the microsomal fraction, but exhibited low activity compared to rat tail arteries prepared in the same manner. PGH-D isomerase was identified in the cytosolic fraction of tail veins. The isomerase was maximally active in the presence of reduced glutathione at pH 7.5-8.0, exhibited a Km for PGH2 of 33 microM, and was inhibited sulfhydryl-directed reagents. The similarities of this enzyme to PGD synthase of the rat cerebral microvasculature are discussed.
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