Abstract
We developed a continuous spectrophotometric assay of the phospholipase A 2 activity specific for choline plasmalogen using rat liver lysoplasmalogenase and horse liver alcohol dehydrogenase as coupling enzymes and Naja naja venom phospholipase A 2 as a source of the phospholipase A 2 activity. In these coupling reactions, choline lysoplasmalogen is hydrolyzed by lysoplasmalogenase to glycerophosphocholine and free aldehyde. The free aldehyde is quantitatively converted to alcohol by alcohol dehydrogenase with the oxidation of NADH. The disappearance of NADH is measured spectrophotometrically at 340 nm. The assay is sensitive to about 0.2 nmol aldehyde produced/ml/min and also is rapid, convenient, and continuous.
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