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Specificity reversal in phospho lipase a 2 ec hydrolysis of lipid mixtures

Biochemical and Biophysical Research Communications 80(2): 424-428
Specificity reversal in phospho lipase a 2 ec hydrolysis of lipid mixtures
The activity and specificity of phospholipase A2 (EC from cobra venom (Naja naja naja) toward binary mixtures of phosphatidylcholine and phosphatidylethanolamine in mixed micelles with the nonionic surfactant Triton X-100 were examined. In mixtures containing 5-50 mol percent phosphatidylcholine, the rate for phosphatidylethanolamine hydrolysis was enhanced greatly over that for phosphatidylcholine. This is in marked contrast to previous studies with individual phospholipid species in mixed micelles where phosphatidylcholine was found to be the preferred substrate and phosphatidylethanolamine was found to be a very poor substrate. Possible explanations for this specificity reversal are considered.

Accession: 006459201

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