Cationic proteins of polymorphonuclear leukocyte lysosomes. I. Resolution of antibacterial and enzymatic activities.
Zeya, H. I. (University of North Carolina, Chapel Hill), and J. K. Spitznagel. Cationic proteins of polymorphonuclear leukocyte lysosomes. I. Resolution of antibacterial and enzymatic activities. J. Bacteriol. 91:750-754. 1966.-A lysosomal fraction from polymorphonuclear (PMN) leukocytes of guinea pig peritoneal exudate was subjected directly to electrophoresis on cellulose acetate paper treated with cetyltrimethyl ammonium bromide. The Iysosomal components resolved into seven bands moving towards the cathode. Assay of the eluted bands showed that the antibacterial activity was distinct from lysosomal enzymes and was associated with three cationic components (bands I, II, and III) which migrated most rapidly towards the cathode, ahead of lysozyme ribonuclease and deoxyribonuclease. Qualitatively, the antibacterial components appeared to be rich in arginine. The antibacterial components were absent in the pherograms of nuclear fractions of PMN leukocytes and in supernatant fractions that remained after lysosomes were removed from cell homogenates by centrifugation at 8,000 x g.
D000818:Animals; D000900:Anti-Bacterial Agents; D001120:Arginine; D002498:Centrifugation; D003851:Deoxyribonucleases; D004586:Electrophoresis; D006168:Guinea Pigs; D066298:In Vitro Techniques; D007477:Ions; D007962:Leukocytes; D008247:Lysosomes; D011506:Proteins; D012260:Ribonucleases; D013347:Subcellular Fractions
D000900:Anti-Bacterial Agents; D007477:Ions; D011506:Proteins; D001120:Arginine; D003851:Deoxyribonucleases; D012260:Ribonucleases