Studies of the Phospholipase A2Activity of Rat Ileal Mucosa

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Abstract
A rapid and simple procedure was used to determine phospholipase A2 activity (EC 3.1.1.4) in rat ileal mucosa. 14C-oleate-labeled Escherichia coli was used as substrate for the phospholipase activity and a 0.45-.mu.m Millipore filter to separate the product of hydrolysis-the 14C-oleic acid-from the unhydrolyzed substrate. The phospholipase A2 activity was optimal at pH 9.8 and at 2 mM Ca2+, but another peak of activity appeared at pH 7.2. In addition, cell fractionation revealed yet another phospholipase A2 activity at pH 5.0 in the absence of Ca2+. More than 1 phospholipase A2 evidently exists in the ileal mucosa and points to the possible use of a simple procedure for studying their distribution and properties.

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