| Literature DB >> 3548813 |
S Forst, J Weiss, P Elsbach, J M Maraganore, I Reardon, R L Heinrikson.
Abstract
The cell-free supernatant of sterile inflammatory peritoneal exudates contains a phospholipase A2 that participates in the digestion of Escherichia coli killed by polymorphonuclear leukocytes or by the purified bactericidal/permeability increasing protein (BPI) of these cells. This phospholipase A2 has been purified, and the sequence of the NH2-terminal 39 amino acids has been determined and compared with sequences of both BPI-responsive and BPI-nonresponsive phospholipases A2 from snake venoms and mammalian pancreas. The high concentration and location of basic residues in the NH2-terminal region is a common feature of BPI-responsive phospholipases A2 and may characterize those phospholipases A2 participating in inflammatory events.Entities:
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Year: 1986 PMID： 3548813 DOI： 10.1021/bi00374a008
Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162