1983 Volume 93 Issue 2 Pages 631-637
Phospholipase A2 of rat liver mitochondria was purified approximately 1, 400-fold by extraction with KCl, and chromatographies on a Sephadex G-75 column and a diacyl-glycerophosphocholine-Sepharose affinity column. The purified enzyme was very labile when incubated either at 37°C or 0°C, and lost its activity within a few hours. Phospholipids or detergents in the solution protected the enzyme against inactivation. The purified phospholipase A2 preferentially hydrolyzed phospha-tidylethanolamine, especially if it contained linoleic acid. The enzyme showed low activity for phosphatidylcholine or phosphatidylinositol.
