RECONSTITUTION OF ACID-DENATURED CATALASE.

@article{Samejima1963RECONSTITUTIONOA,
  title={RECONSTITUTION OF ACID-DENATURED CATALASE.},
  author={Tatsuya Samejima and J. T. Yang},
  journal={The Journal of biological chemistry},
  year={1963},
  volume={238},
  pages={
          3256-61
        }
}

Figures and Tables from this paper

Reversible inactivation and dissociation of yeast hexokinase.

Reconstitution of alkaline-denatured catalase.

Unique oligomeric intermediates of bovine liver catalase

Comparative studies of the effect of NaCl, GdmCl, and urea on BLC show that cation binding to negatively charged groups present in amino acid side chains of the enzyme leads to stabilization of an enzymatically active, folded dimer of BLC.

Alkaline unfolding and salt-induced folding of bovine liver catalase at high pH.

The refolding/reconstitution studies showed that the salt-induced partially folded tetrameric intermediate shows significantly higher efficiency of refolding or reconstitution as compared to alkaline-denatured catalase in the absence of salts.

Solvent perturbation studies of heme proteins and other colored proteins.

The reversible inactivation of rat-liver arginase in low pH.

The renatured enzyme has the same optimum pH and Km as the native enzyme but loses its original activity in the neutral pH region, which makes the renaturation process an apparently first-order reaction.

Denatured hemoproteins as catalysts in lipid oxidation

Urea-denatured hemoprotein possessed increased nonenzymatic activity due to increased exposure of the protein-bound heme, however, peroxidase increased less than catalase which is consistent with the fact that per oxidase is the more heat stable enzyme.

Structure of beef liver catalase.

...