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Synthetic peptide from lipocortin I has no phospholipase A sub(2) inhibitory activity

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 sub(2). Kinetic assays using monomeric and aggregated phospholipids did not reveal any phospholipase A su...

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Bibliographic Details
Published in:FEBS letters 1989-01, Vol.247 (2), p.293-297
Main Authors: van Binsbergen, J, Slotboom, AJ, Aarsman, A J, de Haas, GH
Format: Article
Language:English
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Summary: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 sub(2). Kinetic assays using monomeric and aggregated phospholipids did not reveal any phospholipase A sub(2) inhibitory activity. The peptides did not inhibit phospholipase A sub(2) activity on monolayers of negatively charged substrate and did not prevent phospholipase A sub(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 sub(2).
ISSN:0014-5793