Abstract
Actin has been found in all eukaryotic cells that have been studied in detail and is often the most abundant protein in plant and animal cells. It is less abundant than in the highly specialised cells of striated muscle, which contain around 40 mg/ml actin, but is still the major protein in many cells; the cytoplasm of Acanthamoeba for example, contains 7 mg/ml. Myosin molecules have also been isolated from most types of cell and in each case have been shown to have properties in common with muscle myosin (see Section 4.3). It is probable that small bundles of actin filaments do contract in non-muscle cells in a similar manner to the contraction of myofibrils. But the concentration of myosin in non-muscle cells is very low; the molar ratio of myosin to actin in Acanthamoeba for example, is 1: 200, as compared with 1: 5 in muscle. This fact alone suggests that interfilament sliding, effected by myosin filaments, may not be the dominant function of non-muscle actin filaments.
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Further reading
Reviews
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© 1991 L. A. Amos and W. B. Amos
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Amos, L.A., Amos, W.B. (1991). Actin in Cells: Structural and Contractile Roles. In: Molecules of the Cytoskeleton. Macmillan Molecular Biology Series. Palgrave, London. https://doi.org/10.1007/978-1-349-21739-7_5
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DOI: https://doi.org/10.1007/978-1-349-21739-7_5
Publisher Name: Palgrave, London
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