Abstract
Avian red cells rapidly and extensively metabolize prostaglandin A1 (PGA1) to a polar form that extracts into 80% ethanol and is quantitatively desalted and recovered over a Waters C18 Sep-Pak. This material co-chromatographs with synthetic PGA1-GSH and with the human red cell PGA1 metabolite on cellulose and silica gel thin layer plates and on normal phase high performance liquid chromatography. Quantitation of the amino acid composition by [35S]cysteine incorporation and by fluorometric amino acid analysis of the material eluting from high performance liquid chromatography indicates the presence of PGA1, cysteine, glutamate, and glycine in equimolar ratios. Base sensitivity of the metabolite indicates that it exists largely (80%) in the 9-hydroxyl form. We conclude that the polar metabolite of PGA1 that acts intracellularly to inhibit cyclic AMP efflux by avian red cells is a glutathione conjugate of PGA1.
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