Purification and partial sequence analysis of a 37-kDa protein that inhibits phospholipase A2 activity from rat peritoneal exudates.

摘要: We have purified from rat peritoneal exudates a 37-kDa protein that inhibits phospholipase A2 activity. It is the predominant inhibitor in these preparations and also detected wide variety of cell lines. Levels expression range 0 to 0.5% total protein. In preparations, partially proteolyzed into series lower mass forms, including species at 30, 24, 15 kDa. These fragments all are immunoreactive with an antibody raised against The developed 6-kDa snake venom. primary structure more than half has been deduced by microsequence analysis. sequences closely related its human analogue, which we recently cloned expressed (Wallner, B. P., Mattaliano, R. J., Hession, C., Cate, L., Tizard, R., Sinclair, L. K., Foeller, Chow, E. Browning, J. Ramachandran, K. Pepinsky, (1986) Nature, press), thus infer highly conserved evolutionarily. Properties molecule suggest it member family steroid-induced anti-inflammatory proteins collectively referred as lipocortin.