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April 1, 1994Biochemical JournalOpen Access

Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes

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Authors

IBIngemar BjörkSwedish University of Agricultural SciencesEPEwa PolLund UniversityERElke Raub‐SegallSwedish University of Agricultural Sciences

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Cite This Study

Björk et al. (1994) studied this question.

synapsesocial.com/papers/6a9ea6d0523ea69b6e6a7db3https://doi.org/10.1042/bj2990219
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Also Consider

Synapse has enriched 3 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Papain labelled with fluorescent thiol-specific reagents as a probe for characterization of interactions between cysteine proteinases and their protein inhibitors by competitive titrations1991 · 33 citations
  2. 2Evidence by chemical modification that tryptophan-104 of the cysteine-proteinase inhibitor chicken cystatin is located in or near the proteinase-binding site1990 · 25 citations
  3. 3Demonstration by electrospray mass spectrometry that the peptidyldipeptidase activity of cathepsin B is capable of rat cathepsin B C-terminal processing1993 · 23 citations