title: [Effect of histones on a change in the enzymatic activity of Escherichia coli and Staphylococcus aureus cells].
abstract: Histones have been found to interfere with the permeability of the cellular membranes of Escherichia coli and Staphylococcus aureus, this resulting in the liberation of 14C-amino acids, the UV-absorbing endogenous material, and the products of RNA degradation. Histones, particularly arginine-rich fractions, stimulated the RNAase activity of the bacteria. Histones inhibited the phosphatase activity of E. coli and stimulated that of Staphylococcus aureus. The ATPase activity of the cells increased upon contact with histones. These enzyme systems are presumed to be components of a mechanism whose activity increases upon the action on the cells of factors interfering with the permeability of the membranes so that low-molecular-weight compounds are liberated from the cells. It is possible that the RNAase, ATPase and phosphatase systems repair the pool of low-molecular-weight compounds, thus contributing to the survival of the bacteria.
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D001120:Arginine; D002463:Cell Membrane Permeability / Q000187:drug effects; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology; D006657:Histones / Q000494:pharmacology*; D008239:Lysine; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism; D013211:Staphylococcus aureus / Q000187:drug effects* / Q000201:enzymology
chemical_list: D006657:Histones; D001120:Arginine; D012260:Ribonucleases; D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases; D008239:Lysine
vernacular_title: Vliianie gistonov na izmenenie fermentativnoĭ aktivnosti kletok Escherichia coli i Staphylococcus aureus.