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Specificity reversal in phospho lipase a 2 ec 3.1.1.4 hydrolysis of lipid mixtures


, : Specificity reversal in phospho lipase a 2 ec 3.1.1.4 hydrolysis of lipid mixtures. Biochemical and Biophysical Research Communications 80(2): 424-428

The activity and specificity of phospholipase A2 (EC 3.1.1.4) 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.

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Blomquist C.H.; Kotts C.E.; Hakanson E.Y., 1980: Phospho lipase a 2 inactivation of microsomal 17 beta hydroxy steroid oxido reductase rates of phospho lipid hydrolysis and enzyme inactivation effects of hydrolysis products and properties of the phospho lipase a 2 treated enzyme. Exposure of guinea pig liver microsomes to phospholipase A2 resulted in the nearly complete loss of 17.beta.-hydroxysteroid oxidoreductase (17.beta.-HSD) activity, the time course of which correlated with phospholipid hydrolysis and lysolecithin f...

Adamich, M.; Dennis, E.A., 1978: Specificity reversal in phospholipase A2 hydrolysis of lipid mixtures. Biochemical and Biophysical Research Communications 80(2): 424-428

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