[Permeability of the Escherichia coli outer membrane for ethidium ions and periplasmic alkaline phosphatase during increased synthesis of it].
During augmented synthesis of periplasmic alkaline phosphatase by various strains of Escherichia coli, the outer membrane of bacterial cells becomes permeable for both the enzyme and ethidium ions which do not generally penetrate inside the cells of gram-negative bacteria. In the absence of the lipoprotein in the outer membrane, its permeability for these compounds as well as its sensitivity to membranotropic agents increases, thus testifying to the influence of the lipoprotein upon certain properties of the outer membrane. A competitive interaction was found between the lipoprotein and lipopolysaccharide content in the outer membrane and their content and alkaline phosphatase secretion into the external medium. It is suggested that increased permeability of the E. coli outer membrane during augmented synthesis of the secreted protein is due to impaired biogenesis of membrane components.
Mikhaleva
N I
NI
Zolov
S N
SN
Suzina
N E
NE
Melkozernov
A N
AN
Nesmeianova
M A
MA
D000469:Alkaline Phosphatase / Q000096:biosynthesis / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002463:Cell Membrane Permeability; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D004996:Ethidium / Q000493:pharmacokinetics*; D017136:Ion Transport; D008070:Lipopolysaccharides / Q000378:metabolism; D008074:Lipoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism
D008070:Lipopolysaccharides; D008074:Lipoproteins; D008565:Membrane Proteins; D000469:Alkaline Phosphatase; D004996:Ethidium
Pronitsaemost' vneshneĭ membrany Escherichia coli dlia ionov étidiia i periplazmennoĭ shchelochnoĭ fosfatazy pri ee povyshenoom sinteze.