Cooperative non-specific binding of the cyclic adenosine 3'--5'-monophosphate receptor protein (CRP) from Escherichia coli to double-stranded thymus and lambda pgal DNA

Cooperative non-specific binding of the cyclic adenosine 3'--5'-monophosphate receptor protein (CRP) from Escherichia coli to double-stranded thymus and lambda pgal DNA

Either free or combined with cAMP, CRP binds cooperatively to double-stranded thymus and lambda pgal DNA. The affinity of CRP for both DNAs in these non-specific interactions is increased by cAMP without noticeable change in the degree of cooperativity. Values of the intrinsic association constant,...

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Veröffentlicht in:Comptes rendus hebdomadaires des séances de l'Académie des sciences. Série D. Sciences naturelles 1979-05, Vol.288 (17), p.1327-1330
Hauptverfasser: Blazy, B, Takahashi, M, Baudras, A
Format: Artikel
Sprache:fre
Schlagworte:
Animals
Bacteriophage lambda
Cattle
Cyclic AMP
DNA
DNA, Viral
Kinetics
Protein Binding
Receptors, Cyclic AMP
Thymus Gland
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Zusammenfassung:Either free or combined with cAMP, CRP binds cooperatively to double-stranded thymus and lambda pgal DNA. The affinity of CRP for both DNAs in these non-specific interactions is increased by cAMP without noticeable change in the degree of cooperativity. Values of the intrinsic association constant, cooperativity parameter, and site size of DNA were determined from ultracentrifugal investigations under near-physiological ionic conditions.
ISSN:0567-655X