Acridine Binding by Escherichia coli: pH Dependency and Strain Differences

AUTOR(ES)

Silver, Simon

RESUMO

Acridine dye binding by cells of Escherichia coli has been characterized in terms of a number of parameters. There is a temperature-dependent, readily reversible binding of acriflavine which occurs to a greater extent with acridine-sensitive mutants of E. coli K-12 than with wild-type E. coli B or K-12. There is an essentially irreversible internal binding of acriflavine which occurs when the cellular permeability barriers are destroyed or altered by heat-treatment, elevated pH, treatment with toluene or phenethyl alcohol, or infection with bacteriophage T2 or T4. Both the reversible and the irreversible binding of acridines occurs more effectively with the acridine dye acriflavine than with the related dye proflavine, and still less effectively with 9-aminoacridine and quinacrine. These properties of acridine binding can be correlated with various inhibitory effects of the dyes on the cells.

Documentos Relacionados

• pH homeostasis in Escherichia coli: measurement by 31P nuclear magnetic resonance of methylphosphonate and phosphate.
• Functional lac carrier protein in cytoplasmic membrane vesicles isolated from Escherichia coli: Temperature and pH dependence of dansyl-galactoside binding*
• Dissipation of pH Gradients in Tonoplast Vesicles and Liposomes by Mixtures of Acridine Orange and Anions: Implications for the Use of Acridine Orange as a pH Probe
• Galactoside Accumulation by Escherichia coli, Driven by a pH Gradient
• Induction of SOS functions by alkaline intracellular pH in Escherichia coli.