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- W2000685560 abstract "Actin was isolated and purified from unfertilized sea urchin eggs (Pseudocentrotus depressus and Hemicentrotus pulcherrimus), by a method which utilizes its specific binding activity with myosin from rabbit skeletal muscle. The purified actin exists as a monomer (ovo-G-actin) in salt-free solution. The ovo-G-actin has a sedimentation coefficient of 3.0–3.2 S. On the addition of salt (0.1 M KCl), the ovo-G-actin transforms into a heavy component of 25–28 S, which has a higher viscosity value (ηsp/c) of 0.9 – 2.1 dl/g. The heavy component (ovo-F-actin) was revealed by electron microscopy to be a filament having a diameter of 60–80 Å. The ovo-G-actin in salt-free solution also transforms into the ovo-F-actin on the addition of divalent salts, CaCl2 or MgCl2." @default.
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- W2000685560 date "1970-07-01" @default.
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- W2000685560 title "Polymerization of actin from sea urchin eggs" @default.
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- W2000685560 doi "https://doi.org/10.1016/0014-4827(70)90254-5" @default.
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