Equilibrium studies on the refolding and reactivation of rabbit-muscle aldolase after acid dissociation.

@article{Engelhard1976EquilibriumSO,
  title={Equilibrium studies on the refolding and reactivation of rabbit-muscle aldolase after acid dissociation.},
  author={Martin Engelhard and Rainer Rudolph and R. C. A. Jaenicke},
  journal={European journal of biochemistry},
  year={1976},
  volume={67 2},
  pages={447-53}
}
Dissociation, denaturation, and deactivation of aldolase from rabbit muscle in the acid pH range have been investigated using sedimentation analysis, fluorescence, circular dichroism, and activity tests. Under comparable experimental conditions the pH-dependent profiles of deactivation and denaturation parallel the dissociation of the enzyme. In the range of dissociation at pH4-5tetramers and monomers are in equilibrium. Intrinsic chromophores and far-ultraviolet circular dichroism suggest the… CONTINUE READING
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