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
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man
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container_end_page 5775
container_issue 10
container_start_page 5768
container_title The Journal of biological chemistry
container_volume 264
creator Kramer, R M
Hession, C
Johansen, B
Hayes, G
McGray, P
Chow, EP-C
Tizard, R
Pepinsky, R B
description 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.
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title Structure and properties of a human non-pancreatic phospholipase A sub(2)
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