Arginine-rich proteins of polymorphonuclear leukocyte lysosomes. Antimicrobial specificity and biochemical heterogeneity.
The cationic antibacterial proteins of rabbit PMN lysosomes have been resolved into at least five subfractions. Each of these showed substantial selectivity in its antibacterial action against several pathogenic bacteria, including two smooth and two rough Escherichia coli strains, three Staphylococcus aureus strains, one S. albus, three proteus species and four different cultures of streptococcus. Each of the subfractions possesses a different electrophoretic mobility. Amino acid analyses of the three most cationic components revealed high contents of arginine consistent with their relative electrophoretic mobilities and very high arginine to lysine ratios. Aromatic amino acids were present in very low concentrations in these proteins and their light absorption at 2800 A was correspondingly weak. The evidence of antibacterial specificity, along with marked differences in the arginine-lysine ratios, shows that the cationic antibacterial components of rabbit PMN lysosomes are biologically and chemically heterogeneous.
D000818:Animals; D001120:Arginine / Q000032:analysis*; D001419:Bacteria / Q000187:drug effects*; D001770:Blood Bactericidal Activity; D004586:Electrophoresis; D004926:Escherichia coli / Q000187:drug effects; D007962:Leukocytes / Q000032:analysis*; D008239:Lysine / Q000032:analysis; D008247:Lysosomes / Q000032:analysis*; D010209:Paper; D011511:Proteus / Q000187:drug effects; D011817:Rabbits; D013210:Staphylococcus / Q000187:drug effects; D013291:Streptococcus / Q000187:drug effects; D013395:Sucrose
D013395:Sucrose; D001120:Arginine; D008239:Lysine