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- W1497340069 abstract "The ix86 allele results in Escherichia coli strains that are constitutive for lac operon function and inducer ligands will either repress or induce the enzymes of the operon depending on inducer concentration. The inducer and operator binding properties of the X86 repressor are characterized in vitro. The dissociation constant for the repressor-operator interaction is Kd = 10−15 m. This binding is 40 times tighter than the binding of wild type i+ repressor to operator. The increased affinity is a specific increase in binding to operator because the binding of the X86 repressor to non-operator DNA is unchanged. The binding of the repressor-inducer complex to operator is easily detectable since the ternary complex has a Kd of 10−12 m. The existence of the ternary complex is conclusively demonstrated by measurements of the kinetics of association and dissociation of the repressor-inducer complex to and from the operator. The binding characteristics of the X86 repressor clarify only part of the complex induction pattern. However, in vivo experiments suggest that the repression seen at low inducer concentrations is due to a reversible activation of repressor by inducer." @default.
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- W1497340069 date "1972-12-01" @default.
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- W1497340069 title "The lac repressor-operator interaction" @default.
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- W1497340069 doi "https://doi.org/10.1016/0022-2836(72)90075-7" @default.
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