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Fig. 4. Co-polymerization assays of wild type ${alpha}$ -skeletal-muscle actin and mutants. Samples of an in vitro transcription-translation reaction and ${alpha}$ -actin from rabbit skeletal muscle were mixed, induced to polymerize and pelleted. The amounts of ³⁵S-labeled actin in aggregates (first pellet, before polymerization and without carrier actin), supernatants (did not pellet under any conditions) and final pellets (F-actin, after two rounds of polymerization) were calculated. Mutants with more than 50% of the ³⁵S-labeled actin in filaments were considered to be `wild type'. These include H40Y, M132V, V163L, R183C and D286G. G15R had only 40% polymerization and was considered to be `borderline'. Mutants with less than 50% of ³⁵S-labeled actin in filaments were considered to be impaired in co-polymerization: I64N, N115S, I136M, G182D, R183G, Q263L, G268C, G268R, N280K, I357L, V370F.

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