Lipocortin‐like anti‐phospholipase A2 activity of endonexin

FEBS Letters

Roques, Véronique¹  Fauvel, Josette¹  Chap, Hugues¹  Salles, Jean-Pierre¹  Rochat, Hervé²  Douste-Blazy, Louis¹ 

[1] INSERM Unité 101, Biochimie des Lipides, Hôpital Purpan, 31059 Toulouse Cedex France;INSERM Unité 172, Chimie et Mode d'Action des Toxines Animales, Faculté de Médecine Nord, Boulevard Pierre Dramard, 13326 Marseille Cedex 15, France

关键词: Endonexin;    Lipocortin;    Phospholipase A2;    Ca2+;    Phosphatidylserine;    PLA2;    phospholipase A2;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(87)80754-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown