Novel intestinal phospholipase A2: purification and some molecular characteristics

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Abstract
A new phospholipase A2 from pig ileum which hydrolyzes phosphatidylglycerol at least 200 times more rapidly than phosphatidylcholine was purified to homogeneity. The method involved the following steps: complete delipidation of ileal homogenates by solvent extraction; fractionation and partition between n-butanol and (NH4)2SO4 solution; hydrophobic affinity chromatography on octyl-Sepharose; adsorption chromatography on hydroxylapatite; ion-exchange chromatography on carboxymethyl-Sepharose. Amino acid composition, MW (15,000-16,000), N-terminal amino acid sequence to residue 48, and enzymatic activity on phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and phosphatidylglycerol were determined.