Lipocortin‐like anti‐phospholipase A2 activity of endonexin
- 25 May 1987
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 216 (1) , 45-50
- https://doi.org/10.1016/0014-5793(87)80754-8
Abstract
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 [3H]oleic acid‐labelled Escherichia coli membranes as substrate, endonexin inhibited phospholipase A2 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.Keywords
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