Key result
Addition of DNase I to G-actin decreased the rate of nucleotide exchange from 1.16 x 10^-4 s^-1 to 0.28 x 10^-4 s^-1, suggesting it binds to F-actin before dissociating the monomer.
Population
Globular actin (G-actin) and filamentous actin (F-actin) models
Design
Preclinical
Authors
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May refine actin depolymerization models; leaves open validation in cardiac cytoskeletal contexts.
DNase I decreases the nucleotide exchange rate in G-actin but facilitates a faster exchange rate during the depolymerization of F-actin, suggesting it binds to F-actin before dissociating the monomer.
Sarah E. Hitchcock (1980) studied Actin depolymerization. Deoxyribonuclease I (DNase I) vs. G-actin alone was evaluated on Rate of nucleotide exchange. Addition of DNase I to G-actin decreased the rate of nucleotide exchange from 1.16 x 10^-4 s^-1 to 0.28 x 10^-4 s^-1, suggesting it binds to F-actin before dissociating the monomer.
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