Abstract
Plasmalogens are hydrolyzed by a plasmalogen-selective phospholipase A2. This enzyme, purified from bovine brain, does not require Ca2+ and is localized in cytosol. It has a molecular mass of 39 kDa and is strongly inhibited by glycosaminoglycans, gangliosides, and sialoglycoproteins. These molecules may be involved in the regulation of its enzymic activity. Plasmalogen-selective phospholipase A2 plays an important role in the release of free fatty acids and platelet-activating factor during trauma.
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© 1996 Springer Science+Business Media New York
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Yang, HC., Farooqui, A.A., Horrocks, L.A. (1996). Characterization of Plasmalogen-Selective Phospholipase A2 from Bovine Brain. In: Nigam, S., Kunkel, G., Prescott, S.M. (eds) Platelet-Activating Factor and Related Lipid Mediators 2. Advances in Experimental Medicine and Biology, vol 416. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0179-8_49
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DOI: https://doi.org/10.1007/978-1-4899-0179-8_49
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