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A Fluorescent-Based Assay for Measurement of Phospholipase A2 Activity

A Facile Assay for Cell Sonicates

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Free Radical and Antioxidant Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 108))

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Abstract

Phospholipases A2 (PLA2) catalyze the hydrolysis of the ester bond at the sn-2 position of phospholipids to generate the lysophospholipid and free fatty acid (1). Several classes of PLA2s have been identified (2). They include the low molecular weight-secreted enzymes, which demonstrate a requirement for millimolar concentrations of Ca2+ for full activity and are generally involved in the inflammatory response. The high molecular-weight, cytosolic PLA2s are activated by submicromolar calcium, have specificity for unsaturated fatty acids and arachidonic acid in particular (3,4). The arachidonic acid released can have many direct functions or can serve as a precursor in the formation of the numerous prostaglandin and leukotriene products (5). Thus, it is becoming increasingly clear that this latter class of enzymes are the principle regulators of arachidonic-acid release and therefore play an important role in signal transduction (6).

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© 1998 Humana Press Inc., Totowa, NJ

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Nicotera, T.M., Spehar, G. (1998). A Fluorescent-Based Assay for Measurement of Phospholipase A2 Activity. In: Armstrong, D. (eds) Free Radical and Antioxidant Protocols. Methods in Molecular Biology™, vol 108. Humana Press. https://doi.org/10.1385/0-89603-472-0:211

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  • DOI: https://doi.org/10.1385/0-89603-472-0:211

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-472-3

  • Online ISBN: 978-1-59259-254-8

  • eBook Packages: Springer Protocols

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