Abstract
The subcellular distribution of actin in embryonic chick fibroblasts and brain was examined biochemically. Several gentle extraction procedures, which did not cause the breakdown of muscle filamentous actin, caused the release of large amounts of “cytoplasmic actin” in a monomeric form. This did not behave as a precursor or degradation product of filamentous actin in pulse label experiments and failed to form filaments under the same conditions as muscle actin. However, when it was purified and concentrated it was able to form aggregates which were very similar to paracrystals of muscle filamentous actin. These results suggest that cytoplasmic actin is at a higher concentration than muscle actin before it will polymerize, and that in the cell much of it is either monomeric or in a labile state.
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