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LongText Report for: Washburn_1990_J.Am.Chem.Soc_112_2040

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Kinetic studies of hydrolytic enzymes such as phospholipase A2 (PLA2) have been hampered by the lack of a versatile, sensitive, continuous spectroscopic assay. Spectroscopic assays currently employed either have low sensitivity,* 12 inhibit some PLA2's, use exceedingly poor substrates, require extensive synthesis are incompatible with free thiols, or are not continuous. We report herein a convenient spectrophotometric assay for PLA2 in which the substrate closely resembles a natural phospholipid. In addition, we utilize this approach to design suicide-inhibitory bifunctionally linked substrates (SIBLINKS) which are specific irreversible inhibitors for PLA27 as well as discuss extensions to either assay or modulate the activity of other hydrolytic enzymes.

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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