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Synthetic peptide from lipocortin I has no phospholipase A 2 inhibitory activity
Author(s) -
van Binsbergen J.,
Slotboom A.J.,
Aarsman A.J.,
de Haas G.H.
Publication year - 1989
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(89)81355-9
Subject(s) - phospholipase , chemistry , phospholipase a2 , peptide , biochemistry , phospholipase a , phospholipase a1 , phosphocholine , enzyme , annexin , in vitro , phospholipid , phosphatidylcholine , membrane
Two anti‐inflammatory peptides corresponding to a high amino acid similarity region between lipocortins were synthesized and tested on their ability to inhibit porcine pancreatic phospholipase A 2 . Kinetic assays using monomeric and aggregated phospholipids did not reveal any phospholipase A 2 inhibitory activity. The peptides did not inhibit phospholipase A 2 activity on monolayers of negatively charged substrate and did not prevent phospholipase A 2 action on mixed micelles of 1‐stearoyl‐2‐arachidonoyl‐ sn ‐glycero‐3‐phosphocholine and sodiumdeoxycholate. Ultraviolet difference spectroscopy did not show binding of the peptides to phospholipase A 2 . Therefore we conclude that these anti‐inflammatory peptides do not inhibit pancreatic phospholipase A 2 in vitro, in contrast to the results recently published [(1988) Nature 335,726–730].