Phospholipase A2 activity of lysosomal origin secreted by polymorphonuclear leucocytes during phagocytosis or on treatment with calcium.
1. Peritoneal neutrophil leucocytes, derived from the rabbit, release phospholipase A (EC 3.1.1.4) activity during phagocytosis of complement-coated zymosan particles, or during treatment with Ca2+. This enzyme is able to release [1-14C]oleate from the membrane phospholipids of Escherichia coli. 2. The release of phospholipase A paralleled that of the known lysosomal marker enzymes beta-glucuronidase and lysozyme. The phospholipase A would thus appear to be derived from the lysosomal granules of the cells. 3. The released enzyme is of A2 specificity, has an absolute requirement for divalent cations, and is active over a broad pH range (pH 6-9).
D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D005260:Female; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008247:Lysosomes / Q000187:drug effects / Q000201:enzymology*; D009504:Neutrophils / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology; D010587:Phagocytosis; D010740:Phospholipases / Q000097:blood*; D010741:Phospholipases A / Q000097:blood* / Q000378:metabolism; D054467:Phospholipases A2; D011817:Rabbits; D013379:Substrate Specificity
D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D002118:Calcium