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- W2016469323 abstract "Phospholipid hydrolysis after 30 min exposure to phospholipase A2 or phospholipase C was determined in intact electroplax cells and in the separated conducting and non-conducting membranes. These enzymes, in concentrations of 0.2 and 2.0 mg per ml, caused approximately the same percentage hydrolysis of phosphatidylcholine phosphatidylethanolamine and phosphatidylserine (40–80%); in addition phospholipase C hydrolyzed sphingomyelin. Phospholipase A2 (0.2 and 2.0 mg per ml) caused mitochondrial swelling, and a pinching off of the membrane inpocketings into clusters of small rounded vesicles external to the membrane. Lysophosphatidylcholine (2 mg per ml) caused some vesicular formation, although not nearly as numerous as with phospholipase A2; and no mitochondrial alterations. Phospholipase C (2 mg per ml) caused some mitochondrial swelling, but no vesicle formation. Disruption by phospholipase C of hydrophilic or electrostatic interactions between phospholipids and proteins has less effect on the ultrastructural organization of the membrane than does disruption of hydrophobic interactions by phospholipase A2. The results are discussed in relationship to the fluid mosaic model of membrane organization." @default.
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- W2016469323 date "1976-01-01" @default.
- W2016469323 modified "2023-09-23" @default.
- W2016469323 title "Effect of phospholipases A2 and C on structure and phospholipids of the electroplax" @default.
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- W2016469323 doi "https://doi.org/10.1016/0041-0101(76)90029-5" @default.
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