On the interaction of muscle actin with gadolinium. |
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| Authors: | L C Gershman L A Selden J E Estes |
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| Affiliation: | 1. Research Service U.S. Veterans Administration Medical Center Albany, New York 12208 USA;2. Department of Physiology Albany Medical College Albany, New York 12208 USA |
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| Abstract: | The polymerization of G-actin is prevented by concentrations of gadolinium (GdIII) that exceed the ATP present. Since the susceptibility of G-actin to enzymatic proteolysis is slightly decreased upon addition of GdIII, and the digestibility of F-actin is markedly increased with the same treatment, it appears that actin undergoes GdIII-induced conformational changes. The altered states of actin formed inhibit the GdIII-ATPase activity of myosin, but in all cases, the effect of GdIII on actin is reversed by removal of the trivalent ion with ATP. The reversible changes in conformation induced by GdIII create a state of actin which has properties unlike those of G-actin, F-monomer or F-actin. |
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