Eur J Biochem 1989 Jan 02;1783:657-62. doi: 10.1111/j.1432-1033.1989.tb14495.x.

Tropomyosin in the sea urchin egg cortex.

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Tropomyosin was purified from the Triton-treated cortex fraction of fertilized sea urchin egg. Egg tropomyosin showed characteristics typical of nonmuscle tropomyosins such as low molecular mass, short periodicity of Mg2+-paracrystals, low lysine/arginine ratio, high Mg2+ requirement in binding to F-actin, in addition to the properties of all tropomyosins, namely, stability to high temperature, anomalous migration of SDS/urea gel, dissociation from F-actin under high ionic conditions and very acidic isoelectric point. Co-sedimentation assay of egg tropomyosin with actin in the presence of the previously purified high-molecular-mass actin binding protein (260-kDa protein) showed that these two proteins bind to actin filaments in a non-competitive manner. This suggested that both the proteins play a cooperative role in the formation of actin-filament-based cytoskeletal structure in the cortex.

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Genes referenced: LOC100887844 LOC579470 LOC590297 LOC594261