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Lipocortin‐like anti‐phospholipase A 2 activity of endonexin
Author(s) -
Fauvel Josette,
Salles Jean-Pierre,
Roques Véronique,
Chap Hugues,
Rochat Hervé,
Douste-Blazy Louis
Publication year - 1987
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(87)80754-8
Subject(s) - egta , phosphatidylserine , chemistry , phospholipase a2 , biochemistry , annexin , size exclusion chromatography , chromatography , affinity chromatography , calcium , substrate (aquarium) , polyacrylamide gel electrophoresis , membrane , phospholipid , enzyme , biology , in vitro , ecology , organic chemistry
Endonexin (protein II, 32.5 kDa) has been purified to homogeneity from bovine liver in the following steps: selective extraction by EGTA from membranes precipitated with Triton X‐100/calcium; chromatography on DEAE‐TSK 545 at pH 7.0, endonexin being eluted at 0.1 M NaCl; affinity chromatography on polyacrylamide‐immobilized phosphatidylserine; gel filtration on TSK 3000. The amino acid composition was essentially similar to that previously reported. Using [ 3 H]oleic acid‐labelled Escherichia coli membranes as substrate, endonexin inhibited phospholipase A 2 from pig pancreas. Maximal inhibition was 55 and 70%, whereas 50% inhibition occurred at 480 and 120 nM endonexin and lipocortin II, respectively. These data could be related to common features shared by both lipocortins/calpactins and endonexin, i.e. the presence of a consensus sequence and the ability to bind to anionic phospholipids in a calcium‐dependent manner.