Zinc metalloenzyme properties of active and latent collagenase from rabbit bone.

@article{Swann1981ZincMP,
  title={Zinc metalloenzyme properties of active and latent collagenase from rabbit bone.},
  author={J C. Swann and J. Joshua Reynolds and W A Galloway},
  journal={The Biochemical journal},
  year={1981},
  volume={195 1},
  pages={41-9}
}
1. Inhibition of collagenase from rabbit bone cultures by the chelating agents 1,10-phenanthroline and EDTA is almost completely reversed by Zn2+; other metal cations are less effective in reversing the inhibition. Optimal restoration of activity is achieved at Zn2+ concentrations below that of the chelator, but excess of Zn2+ is inhibitory. 2. Prolonged incubation of collagenase with either chelator causes irreversible inactivation. This inactivation is prevented by Zn2+ at the same… CONTINUE READING