Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins.

@article{Turk1995RegulationOT,
  title={Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins.},
  author={Boris Turk and Joseph G. Bieth and Ingemar Bj{\"o}rk and Iztok Dolenc and Dŭsan Turk and Nina Gunde Cimerman and Janko Kos and Ana Miki{\'c} {\vC}oli{\'c} and Veronika Stoka and Vito Turk},
  journal={Biological chemistry Hoppe-Seyler},
  year={1995},
  volume={376 4},
  pages={225-30}
}
The kinetics of pH-induced inactivation of human cathepsins B and L was studied by conventional and stopped-flow methods. The inactivation of both enzymes was found to be an irreversible, first-order process. The inactivation rate constants increased exponentially with pH for both enzymes. From log kinac vs pH plots, 3.0 and 1.7 protons were calculated to be desorbed for pH-induced inactivation of cathepsins L and B. Cathepsin B was thus substantially more stable than cathepsin L (approximately… CONTINUE READING

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