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• W1506397261 abstract "The interaction between the four binding sites (two A sites and two B sites) of the regulatory subunit dimer of protein kinase I (RI2) was studied. The rate of association of c[3H]AMP to site B was slower when site A had already been occupied. Occupation of site A also retarded the rate of dissociation of c[3H]AMP from site B. This site A-B interaction was intrachain since it was observed also for a monomeric fragment of RI2. Thus, each monomer of RI2 must have one A site and one B site. Quantitative analysis of the rate constants for cAMP binding to variously liganded RI2 suggested little or no thermodynamic coupling between site A and B. This conclusion was supported by equilibrium binding data. Occupation of one A site retarded the dissociation of c[3H]AMP from the A site of the other subunit (interchain interaction). The rate kinetic constants as well as equilibrium binding data indicated a positively cooperative site A-A interaction. The interaction between cAMP and either site was enthalphy-driven (25 degrees C), the process being accompanied by a loss of entropy. The thermodynamic parameters did not support the occurrence of an abrupt conformational change at a certain level of ligandation of RI2. Half-maximal saturation of either site occurred at 1-2 nM cAMP (37 degrees C, pH 7.0, 0.15 M KCl). The concentration of RI2 did not detectably influence any binding parameters. Aging of RI2 produced a form with minimally, if at all, altered Mr, but which showed a more rapid release of c[3H]AMP bound to site B." @default.
• W1506397261 created "2016-06-24" @default.
• W1506397261 creator A5031838194 @default.
• W1506397261 creator A5066573040 @default.
• W1506397261 date "1984-02-01" @default.
• W1506397261 modified "2023-10-18" @default.
• W1506397261 title "Characterization of the interchain and intrachain interactions between the binding sites of the free regulatory moiety of protein kinase I." @default.
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• W1506397261 doi "https://doi.org/10.1016/s0021-9258(17)43351-5" @default.
• W1506397261 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6321466" @default.
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