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• W2000593758 abstract "Previous conflicting reports suggest that DNase-I binds F-actin with either equal or drastically different KD values compared to G-actin. We developed a high-throughput DNase-I inhibition assay to determine the KD of DNase-I for F-actin. We confirmed that phalloidin-stabilized F-actin is protected from depolymerization by DNase-I and that the critical concentration at the pointed end of phalloidin–F-actin is 45.5 ± 13.9 nM. We found that DNase-I inhibition by actin follows ultrasensitive mechanics. Using varying lengths of gelsolin-capped phalloidin–F-actin, we concluded that the affinities of DNase-I for G- and the pointed end subunits of F-actin are almost indistinguishable, such that DNase-I may not distinguish between G- and F-actin conformations." @default.
• W2000593758 created "2016-06-24" @default.
• W2000593758 creator A5002226707 @default.
• W2000593758 creator A5034401392 @default.
• W2000593758 date "2007-05-01" @default.
• W2000593758 modified "2023-10-02" @default.
• W2000593758 title "A high-throughput assay shows that DNase-I binds actin monomers and polymers with similar affinity" @default.
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• W2000593758 doi "https://doi.org/10.1016/j.ab.2007.02.027" @default.
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