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  • Title: Structural and functional properties of a phospholipase A2 purified from an inflammatory exudate.
    Author: Forst S, Weiss J, Elsbach P, Maraganore JM, Reardon I, Heinrikson RL.
    Journal: Biochemistry; 1986 Dec 30; 25(26):8381-5. PubMed ID: 3548813.
    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.
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