Novel intestinal phospholipase A2: purification and some molecular characteristics.
We purified to homogeneity a new phospholipase A2 from pig ileum which hydrolyzes phosphatidylglycerol at least 200 times more rapidly than phosphatidylcholine. The method involved the following steps: (1) complete delipidation of ileal homogenates by solvent extraction; (2) fractionation and partition between n-butanol and (NH4)2SO4 solution; (3) hydrophobic affinity chromatography on octyl-Sepharose; (4) adsorption chromatography on hydroxylapatite; (5) ion-exchange chromatography on carboxymethyl-Sepharose. Amino acid composition, molecular weight (15 000-16 000), N-terminal amino acid sequence to residue 48, and enzymatic activity on phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and phosphatidylglycerol were determined.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D007422:Intestines / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D010715:Phosphatidylglycerols / Q000378:metabolism; D010740:Phospholipases / Q000302:isolation & purification*; D010741:Phospholipases A / Q000302:isolation & purification*; D054467:Phospholipases A2; D013552:Swine
D000596:Amino Acids; D010715:Phosphatidylglycerols; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2