G-actin


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G-ac·tin

the globular (G) subunit of the actin molecule, having a molecular weight 42 kD; it is soluble in dilute salt, polymerizing to F-actin when the ionic strength is increased.

G-ac·tin

(akt'in)
The globular (G) subunits of the actin molecule, having a molecular weight of 57,000 and containing one molecule of adenosine triphosphate.
References in periodicals archive ?
Accurate quantitation of native Gc in serum and estimation of endogenous Gc: G-actin complexes by rocket immunoelectrophoresis.
Moreover, this effect occurred regardless of the divalent cation (i.e., [Mg.sup.2+], [Ca.sup.2+], or none) bound to the high-affinity binding site (HAS) of the G-actin monomer.
Moreover, we have systematically investigated the effect of the divalent cation (i.e., [Mg.sup.2+], [Ca.sup.2+], or none) bound to the HAS of the G-actin molecule in terms of the mechanical properties and 3-D structure of the resulting F-actin filaments (i.e., polymerized in the presence of 100 mM KCl).
Previously it was mentioned the F-actin and G-actin. Since the cytoskeleton is a product of evolution, this is constituted by three main kinds of filamentous polymers: F-actin, microtubules and neuro- filaments.
Tiago et al., "Decavanadate interactions with actin: inhibition of G-actin polymerization and stabilization of decameric vanadate," Journal of Inorganic Biochemistry, vol.
(1,2) Soon after its discovery, it was found that a monomeric globular actin (G-actin) with the molecular mass of 42 kDa contains one ATP and that the polymerization of monomeric actin (globular actin, G-actin) to form filaments (filamentous actin, F-actin) is dependent on [Mg.sup.2+] and KCl, and facilitates the hydrolysis of ATP.
These propelling forces in molecular scale originate from rapid assembly and disassembly of globular G-actin monomers to filamentous F-actin polymers [3].
Structural and Phylogenetic Analysis of the g-Actin Encoding Gene from the Penicillin-Producing Fungus Penicillium chrysogenum.
cholerae toxin ([MARTX.sub.vc]) covalently binds to G-actin and F-actin, and causes actin depolymerization, which leads to cell rounding (Kudryashov et al.