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• W2329881036 abstract "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 15-fold at pH 7.0 and 37 degrees C). Cathepsin B was efficiently inhibited by cystatin C at pH 7.4, whereas the inhibition by stefin B and high molecular weight kininogen was only moderate. In contrast, cathepsin L was efficiently inhibited by both chicken cystatin and stefin B at this pH kass approximately 3.3 x 10(7) m-1 s-1)." @default.
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• W2329881036 date "1995-01-01" @default.
• W2329881036 modified "2023-10-18" @default.
• W2329881036 title "Regulation of the Activity of Lysosomal Cysteine Proteinases by pH-Induced Inactivation and/or Endogenous Protein Inhibitors, Cystatins" @default.
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• W2329881036 doi "https://doi.org/10.1515/bchm3.1995.376.4.225" @default.
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