A prostaglandin dehydrogenase (sp act, 15 units/mg protein) was isolated from the canine myocardium. The enzyme oxidized the 15-hydroxy group of most prostaglandins tested except for PGBs and PGA2 which were poor substrates. It required NAD and intact sulfhydryl groups. Its activity was enhanced by cyclic 3′,5′-AMP at low concentrations (10-10 to 10-7 M) and inhibited by CaCl2. The significance of these findings for the control of myocardial prostaglandin levels is discussed.
|Original language||English (US)|
|Number of pages||5|
|Journal||Proceedings of the Society for Experimental Biology and Medicine|
|State||Published - Apr 1973|
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