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J Bacteriol. 1968 February; 95(2): 333-339
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Acridine Binding by Escherichia coli: pH Dependency and Strain Differences

Simon Silver, Elaine Levine and Philip M. Spielman

Department of Biology, Washington University, St. Louis, Missouri 63130
Virus Laboratory, University of California, Berkeley, California 94720

ABSTRACT

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.


J Bacteriol. 1968 February; 95(2): 333-339
Copyright © 1968 American Society for Microbiology. All Rights Reserved.







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