We have developed a method for the isolation of a brain subcellular fraction enriched in both highly aggregated polyribosomes and cytoskeletal proteins. This method is based on gentle homogenization of brain tissue and low speed centrifugation. The mechanism of association of polyribosomes to cytoskeletal structures has been studied by in vitro treatment of this fraction with polyribosome-disaggregating agents. RNase and EDTA, while succeeding in completely disrupting them into monosomes or subunits, did not release them from cytoskeleton. Puromycin showed no noticeable effect.
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