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.

Samankaltaisia teoksia

• Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases.
  Tekijä: Pol, E, et al.
  Julkaistu: (1995)
• Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin.
  Tekijä: Lindahl, P, et al.
  Julkaistu: (1992)
• 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.
  Tekijä: Lindahl, P, et al.
  Julkaistu: (1992)
• Importance of the evolutionarily conserved glycine residue in the N-terminal region of human cystatin C (Gly-11) for cysteine endopeptidase inhibition.
  Tekijä: Hall, A, et al.
  Julkaistu: (1993)
• 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.
  Tekijä: Björk, I, et al.
  Julkaistu: (1994)