Abstract
Summary Reaction between N-ethyl-5-isoxazolium-3-sulfonate, a reagent specific for carboxylate residues, and pancreatic porcine phospholipase A 2 results in complete elimination of enzymatic activity. The modification reaction is prevented in presence of hexadecylphosphorylcholine and N-palmitoylaminoethylphosphorylcholine acting as reversible phospholipase A 2 inhibitors. The decrease of enzymatic activity correlates with the modification of a single carboxylate residue. The possible catalytic role of the carboxylate is discussed and a model for the active-site is proposed.
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