A study of the action of the cationic proteins from rabbit polymorphonuclear leucocytes on the staphylococcal cell membrane.
The inhibitory effect of cationic proteins from rabbit polymorphonuclear leucocytes on the oxidation of NADH by staphylococcal membrane preparations is described. Both cyanide and haematin are shown to interfere with the inhibitory process, by different mechanisms. Other authors have shown that glucose repressed staphylococci are diverted to a fermentative mode of metabolism. These findings were confirmed by demonstrating that membrane preparations from staphylococci grown in the presence of glucose have diminished cytochrome and succinic dehydrogenase levels. From a comparison of the effect of the cationic proteins on NADH oxidation in membrane preparations from organisms grown normally and under conditions of glucose repression, and from knowledge of the different susceptibility to the cationic proteins of the two types of organisms, it is suggested that the cationic proteins exert their bactericidal action on staphylococci following an energy dependent binding to the membrane.
D001798:Blood Proteins / Q000494:pharmacology*; D002462:Cell Membrane / Q000032:analysis / Q000187:drug effects / Q000201:enzymology; D003486:Cyanides / Q000494:pharmacology; D003580:Cytochromes / Q000032:analysis; D006418:Heme / Q000494:pharmacology; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis; D009504:Neutrophils / Q000032:analysis; D011485:Protein Binding; D013211:Staphylococcus aureus / Q000187:drug effects; D013385:Succinate Dehydrogenase / Q000032:analysis; D013997:Time Factors
D001798:Blood Proteins; D003486:Cyanides; D003580:Cytochromes; D006418:Heme; D013385:Succinate Dehydrogenase; D009247:NADH, NADPH Oxidoreductases