Abstract
A phospholipase A 2 has been found in association with several commercial human and bovine serum albumin preparations. Activity is maximal between pH 6.0 and 8.0 and has been demonstrated using as substrates [1- 14C]oleate-labeled Escherichia coli after autoclaving the labeled bacteria, and purified [1- 14C]fatty acid-labeled phosphatidylethanolamine. The rates of breakdown of the major E. coli phospholipids were roughly comparable. The phospholipase activity seems distinct from triglyceride-splitting activities in association with albumin, described by others. The presence of phospholipase A in serum albumin preparations, often used in experiments with cells and tissues in vitro, may influence the results.
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