Rabbit skeletal muscle F-actin can be stable at low ionic strength, provided trace amounts of Ca2+ are absent
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference11 articles.
1. Dual effect of Ca2+ on ultrasonic ATPase activity and polymerization of muscle actin
2. Regulation in molluscan muscles
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4. Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle
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1. A Conformational Change in the Actin Subunit Can Change the Flexibility of the Actin Filament;Journal of Molecular Biology;1993-07
2. Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion;European Journal of Biochemistry;1993-02
3. Characterization of yeast-expressed beta-actins, site-specifically mutated at the tumor-related residue Gly245;European Journal of Biochemistry;1992-07
4. Divalent cation binding to the high- and low-affinity sites on G-actin;Biochemistry;1987-10
5. Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin.;Journal of Biological Chemistry;1986-08
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