Structure and properties of a human non-pancreatic phospholipase A sub(2)

Structure and properties of a human non-pancreatic phospholipase A sub(2)

The authors have purified a human non-pancreatic phospholipase A sub(2) that is present in platelets and is enriched in rheumatoid synovial fluid. The enzyme is calcium-dependent, has a pH optimum of 8-10, and shows a striking preference for substrate presented in the form of Escherichia coli) membr...

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Veröffentlicht in:The Journal of biological chemistry 1989-01, Vol.264 (10), p.5768-5775
Hauptverfasser: Kramer, R M, Hession, C, Johansen, B, Hayes, G, McGray, P, Chow, EP-C, Tizard, R, Pepinsky, R B
Format: Artikel
Sprache:eng
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man
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Zusammenfassung:The authors have purified a human non-pancreatic phospholipase A sub(2) that is present in platelets and is enriched in rheumatoid synovial fluid. The enzyme is calcium-dependent, has a pH optimum of 8-10, and shows a striking preference for substrate presented in the form of Escherichia coli) membranes. In the E. coli phospholipase A sub(2) assay the phospholipase exhibits an apparent specific activity of 300 mu mol/mg/min.
ISSN:0021-9258