Abstract
Rat tail vein homogenates, microsome and high speed supernatant fractions were incubated with [1- 14C]prostaglandin endoperoxide (PGH 2) and products separated and identified by radio-thinlayer chromatography. PGI 2 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 maximally active in the presence of reduced glutathione at pH 7.5–8.0, exhibited a K m for PGH 2 of 33 μM, 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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