A comparative study of proteolytic enzymes and their inhibitors in three human leukemic lymphoid cell populations has been carried out. The lysates of all lymphoid cells contained cathepsins D, B, L and H as well as serine trypsin-like proteinases, several aminopeptidases, dipeptidyl aminopeptidase IV and plasminogen activator (urokinase type). The activities of individual proteinases and their ratios in all cell types under study varied essentially, suggesting that lymphoid cells with different functions have different sets of proteolytic enzymes. FPLC chromatography of the lysates revealed the presence of inhibitors of cysteine and serine trypsin-like proteinases. The procedure for isolation of cathepsins D, B, L and H and of their inhibitors has been proposed and partially purified protein preparations obtained. Some properties of cathepsins B and L and those of their inhibitor have been examined.

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