Abstract
Partially purified rhesus monkey lung 15-hydroxyl prostaglandin dehydrogenase (15-OH PGDH) catalyzed the NAD-dependent oxidation of prostacyclin (PGI 2) and 6-keto-PGF 1a to 6,15-diketo-PGF 1a. The product was identified by gas chromatography-mass spectroscopy. Prostacyclin was oxidized four to six times faster than 6-keto-PGF 1a under identical reaction conditions, suggesting that the metabolism of prostacyclin probably proceeds through a bicyclic 15-keto intermediate before chemically decomposing to the final stable product, 6,15-diketo-PGF 1a. Prostacyclin has a good affinity for the 15-OH PGDH enzyme. A Lineweaver-Burke plot gave an apparent K m value of 7.4 μ m, which compares very favorably with the K m values for PGE 1 and PGE 2.
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