Abstract
The role of proteasomes, particles with latent multicatalytic proteinase, in ATP‐dependent proteolysis in rat reticulocyte extracts was examined. Removal of proteasomes from the extracts by immunoprecipitation caused almost complete inhibition of ATP‐dependent degradation of [3H]methylcasein, without affecting ATP‐independent proteolysis. Peptide fragments of [3H]casein, obtained by cyanogen bromide cleavage, were rapidly degraded in an ATP‐independent fashion and this activity was not affected by removal of the proteasomes. These results suggest that proteasomes are involved in ATP‐dependent proteolysis in the extracts and that they catalyze the initial cleavage of large proteins.