Proteolytically active complexes of cathepsin L and a cysteine proteinase inhibitor; purification and demonstration of their formation in vitro Academic Article uri icon

abstract

  • Proteolytically active complexes of the proteinase cathepsin L, with an endogenous inhibitor of cysteine proteinases, were purified from sheep liver. The complexes were active against the synthetic substrate Z-Phe-Arg-NHMec and also the proteins azocasein and gelatin. The composition of the complexes was demonstrated by Western blotting, after reducing and nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis with monospecific antibodies raised against purified sheep liver cathepsin L and purified sheep liver cysteine proteinase inhibitor (probably stefin B). Similar complexes could be formed in vitro, by coincubation of purified sheep liver cathepsin L with the purified sheep liver cystatin at a pH of 5.5 or higher.

publication date

  • May 1992

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