Multiple forms of porcine pancreatic phospholipase A₂: Isolation and specificity

Abstract

Abstract Porcine pancreatic phospholipase A 2 was purified from commercial pancreatin by a method involving heat denaturation, trichloroacetic acid precipitation, and DEAE‐cellulose chromatography. Assaying the eluate of the chromatography step by a new titrimetric method using vegetable lecithin‐albumin emulsion as the substrate, several species of phospholipase A were found. Some of these went undetected when the conventional egg yolk emulsion assay was used. Two phospholipases A 2 were isolated in a homogeneous form and shown to have similar chemical and physical properties. Catalytic specificity of the two enzymes differs remarkably toward lecithins in different emulsified states.