Conversion of ATP‐actin to ADP‐actin reverses the affinity of monomeric actin for Ca2+ vs Mg2+
- 8 June 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 217 (1) , 89-93
- https://doi.org/10.1016/0014-5793(87)81249-8
Abstract
Monomeric ATP-actin binds Ca2+ 3–4-times more strongly than Mg2+ at pH 8. On conversion of G-ATP-actin to G-ADP-actin, the relative affinity of actin for the divalent cations is reversed, so that Mg2+ is bound 6-times more strongly than Ca2+. The dissociation rate constant of Ca2+ from Ca-ADP-actin is 50-fold higher than that for Ca2+ from Ca-ATP-actin, suggesting that this reversal of divalent cation affinities is due primarily to a higher equilibrium dissociation constant for Ca-ADP-actin. These results demonstrate an interaction between the actin-bound nucleotide and divalent cation or their binding sites.Keywords
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