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The membrane attack complex of complement and its precursor proteins lack phospholipase activity
Authors:Carl-Wilhelm Vogel  Andreas Plückthun  Eckhard R. Podack  Edward A. Dennis  Hans J. Müller-Eberhardb
Affiliation:2. Department of Molecular Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037, U.S.A.;3. Department of Chemistry, University of California at San Diego, La Jolla, California 92093, U.S.A.
Abstract:The membrane attack complex of human complement and its highly purified precursor proteins have been analyzed for phospholipase activity. Using three different sensitive assays, phospholipase a1, A2, C or D activity could not be detected. Based on the sensitivity of the assays employed, these results indicate the complement-mediated membrane damage is not enhanced by covalent breakdown of membrane phospholipids, but is entirely caused by physical action of the membrane attack complex. The results also imply that the putative serine esterase sites of C6 and C7 are not acting on phospholipids.
Keywords:MAC  membrane attack complex  poly C9  polymerized C9  DFP  diisopropylfluorophosphate  TLCK  PMSF  phenylmethylsulfonylfluoride  pAPMSF  TLC  thin layer chromatography  FID  flame ionization detection
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