The chromatographic support containing monolayers of phospholipids offers novel modes in analyzing and separating proteins. The polar choline headroups on immobilized phosphatidylcholine were used for the affinity purification of phospholipase A (PLA). The purification process involves removing the contaminating proteins with detergent additives to the elution buffer such as short-chain alkylsulfonates. The lipid-bound PLA was eluted with acetonitrile or octyllysophosphatidylcholine. The purity of PLA was approximately 70% based on densitometric scans ofel electrophoresis. These results suggest that the lipid-immobilized chromatography may be applied to develop purification methods for PLA, enzymes, and membrane proteins obtained from diverse cells.
