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- W1992695087 abstract "The dissociation of the complex between 1:N6-ethenoadenosine 5′-triphosphate (ɛP) and G-actin was initiated by dilution to concentrations between 1 μM and 5 nM and monitored by the fluorescence change of ɛP. The results were quantitatively explained by a two-step mechanism: a reversible dissociation of the actin · nucleotide complex followed by a fast irreversible inactivation of nucleotide-free G-actin. Under normal conditions (0.8 mM CaCl2, pH 8.2, 21 °C), the rate-limiting step was the dissociation of the nucleotide· G-actin complex. The half-time of the dissociation of ɛP from G-actin was 290 s as compared to only 13 s for the following denaturation step of nucleotide-free actin. 1 mM EDTA highly accelerated the dissociation step and, regardless of its concentration, the complex dissociated quantitatively within 1 min. Addition of Ca2+ within 20 s after EDTA addition induced a re-association of ɛP with nucleotide-free but still native G-actin. This reversal was kinetically resolved by means of a multimixing stopped-flow apparatus. The association rate constant was 6 × 106 M−1 s−1. From the association and dissociation rate constant, a value of 2.5 × 109 M−1 was calculated for the binding constant of ɛP to G-actin. The binding constant of ATP (1.4 × 1010 M−1) was derived from the relative binding constant of ɛP and ATP as determined by fluorescence titration of ɛP · G-actin with ATP. These binding constants are 103–104 times higher than values reported earlier on the basis of more indirect data." @default.
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- W1992695087 date "1977-04-01" @default.
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- W1992695087 title "Association Kinetics and Binding Constants of Nucleoside Triphosphates with G-Actin" @default.
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- W1992695087 doi "https://doi.org/10.1111/j.1432-1033.1977.tb11385.x" @default.
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