Abstract
The distribution and some properties of the liver cell cathepsins have been studied. Cathepsins A, B and C as well as another type of protease were demonstrated in nuclei and the mitochondrial fraction of liver cells, and saline and HCl extracts of all types of aqueous as well as non-aqueous preparations of nuclei that were investigated showed high degrees of proteolytic activity. This makes the characterization of protein fractions isolated from the nuclei somewhat hazardous, owing to the difficulty of avoiding enzymatic degradation during fractionation procedures. NaCl and HCl extracts from Behrens' type nuclei showed even higher proteolytic activity than corresponding extracts of nuclei isolated at pH 5.8 in aqueous media. This finding constitutes some evidence for the natural occurrence of cathepsins within the nucleus of the living cell.
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