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.

Ítems similars

• Characterization by rapid-kinetic and equilibrium methods of the interaction between N-terminally truncated forms of chicken cystatin and the cysteine proteinases papain and actinidin.
  per: Lindahl, P, et al.
  Publicat: (1992)
• Probing the functional role of the N-terminal region of cystatins by equilibrium and kinetic studies of the binding of Gly-11 variants of recombinant human cystatin C to target proteinases.
  per: Björk, I, et al.
  Publicat: (1995)
• The N-terminal region of cystatin A (stefin A) binds to papain subsequent to the two hairpin loops of the inhibitor. Demonstration of two-step binding by rapid-kinetic studies of cystatin A labeled at the N-terminus with a fluorescent reporter group.
  per: Estrada, S., et al.
  Publicat: (2000)
• Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin.
  per: Lindahl, P, et al.
  Publicat: (1992)
• Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases
  per: Pol, Ewa, et al.
  Publicat: (2001)