Journal of Supramolecular Structure · 1976 · 394 citations · 24 references
Life SciencesBiochemistryCell BiologyCell BiophysicsCell PhysiologyCytoskeletonActin FilamentsCytoskeletal ArchitectureCytoskeletal Associated ProteinsCytoskeletal OrganizationCytoskeleton BiochemistryIntermediate FilamentsCytoskeletal ElementsCytoskeletal Protein StructureDetergent TreatmentGel ElectrophoresisSupramolecular Interactions
Treatment of chick embryo fibroblasts with 0.5% Triton X-100 extracts most of the cell protein, leaving an organized part of the cell structure attached to the tissue culture dish. This "Triton cytoskeleton" consists largely of intermediate-sized filaments and bundles of microfilaments. SDS polyacrylamide gel electrophoresis reveals that this cytoskeleton is made up of three main proteins. One protein component is 42,000 daltons and co-migrates with muscle actin. The other two components are 52,000 and 230,000 daltons and remain quantitatively associated with the cytoskeleton during the detergent extraction. The possible identity of these three protein components and their organization into a supramolecular structure is discussed.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations