Abstract
The interaction of tritiated prostaglandin E1 (3H-PGE1) with various constituents of human blood was examined by equilibrium dialysis and incubation experiments. Plasma bound 3H-PGE1 weakly, apparently due to an interaction with serum albumin. Blood cells and plasma globulins did not interact with PG. When albumin and other proteins were precipitated by ethanol, as a preliminary stage of extracting PG from plasma, the recoveries of added PGs were poor. Addition of acid and non-precipitating amounts of ethanol (40–50%) to the plasma allowed quantitative extraction of added PGE, F, and A compounds into chloroform.