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Diacylglycerol lipase activity in human platelet intracellular and surface membranes
Author(s) -
Authi Kalwant S.,
Lagarde Michel,
Crawford Neville
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80239-8
Subject(s) - diacylglycerol kinase , diacylglycerol lipase , egta , membrane , intracellular , chemistry , biochemistry , lipase , arachidonic acid , oleic acid , enzyme , substrate (aquarium) , linoleic acid , palmitic acid , enzyme assay , fatty acid , biology , protein kinase c , calcium , organic chemistry , ecology
Diacyl glycerol lipase activity has been examined of intracellular and surface membranes isolated from human blood platelets by free flow electrophoresis. Enzyme activity is present on both membranes but is activated at different substrate concentrations ( K m 14 μM and 140 μM for intracellular and surface membrane, respectively). Both enzyme activities are stimulated by EGTA and GSH, and inhibited by added Ca 2+ . The specificity of the intracellular membrane enzyme has been investigated using a range of diacylglycerol substrates differing only in their ‘2’ position fatty acid. Arachidonic acid is clearly the preferred ‘2’ position moiety with activities towards eicosatrienoic, linoleic, oleic and palmitic acid‐containing substrates, all substantially lower.