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About 50 protein fractions with molecular mass 15-158 kDa were detected in purified mitochondria isolated from rat liver homogenate after two-dimensional electrophoresis performed as described by O'Farrell. Individual spots, corresponding to proteins of inner mitochondrial membrane, disappeared from electrophoregrams as a result of incubation of the isolated mitochondria at 37 degrees and pH 7.5. Degradation of these proteins was augmented if ATP was added into incubation mixtures. Intrinsic proteolytic activity occurred in rat liver mitochondria as shown by these and previously obtained data.
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