The membrane attack complex of complement and its precursor proteins lack phospholipase activity.
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.
D002855:Chromatography, Thin Layer; D015938:Complement Membrane Attack Complex; D003165:Complement System Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D005410:Flame Ionization; D006461:Hemolysis; D006801:Humans; D010740:Phospholipases / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D011498:Protein Precursors
D015938:Complement Membrane Attack Complex; D010743:Phospholipids; D011498:Protein Precursors; D003165:Complement System Proteins; D010740:Phospholipases