Key result
Displacement of actin-bound nucleotides by ATP in rabbit skeletal muscle G-actin is biphasic with Ca2+ and a slow first-order process with low Mg2+.
The study proposes a mechanism for nucleotide displacement in monomeric actin involving two forms of an actin-ADP complex whose ratio is influenced by metal binding.
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No immediate clinical implications from rabbit skeletal actin data; leaves open metal-dependent nucleotide exchange mechanisms for cardiac research.
Frieden et al. (1988) studied this question. Displacement of actin-bound nucleotides by ATP in rabbit skeletal muscle G-actin is biphasic with Ca2+ and a slow first-order process with low Mg2+.
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