Washburn_1990_J.Am.Chem.Soc_112_2040

Reference

Title : Novel General Approach for the Assay and Inhibition of Hydrolytic Enzymes Utilizing Suicide-Inhibitory Bifunctionally Linked Substrates (SIBLINKS): Exemplified by a Phospholipase A2 Assay - Washburn_1990_J.Am.Chem.Soc_112_2040
Author(s) : Washburn WN , Dennis
Ref : Journal of the American Chemical Society , 112 :2040 , 1990
Abstract :

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.

PubMedSearch : Washburn_1990_J.Am.Chem.Soc_112_2040
PubMedID:
Gene_locus related to this paper: human-PLA2G7

Related information

Substrate DNPG
Gene_locus human-PLA2G7

Citations formats

Washburn WN, Dennis (1990)
Novel General Approach for the Assay and Inhibition of Hydrolytic Enzymes Utilizing Suicide-Inhibitory Bifunctionally Linked Substrates (SIBLINKS): Exemplified by a Phospholipase A2 Assay
Journal of the American Chemical Society 112 :2040

Washburn WN, Dennis (1990)
Journal of the American Chemical Society 112 :2040