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.

Lignende værker

• Inactivation of papain by antithrombin due to autolytic digestion: a model of serpin inactivation of cysteine proteinases.
  af: Björk, I, et al.
  Udgivet: (1998)
• Papain labelled with fluorescent thiol-specific reagents as a probe for characterization of interactions between cysteine proteinases and their protein inhibitors by competitive titrations.
  af: Lindahl, P, et al.
  Udgivet: (1991)
• Interaction of chicken cystatin with inactivated papains.
  af: Björk, I, et al.
  Udgivet: (1989)
• Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases.
  af: Pol, E, et al.
  Udgivet: (1995)
• 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.
  af: Björk, I, et al.
  Udgivet: (1994)