Denaturation of horseradish peroxidase with urea and guanidine hydrochloride.
Favourable effects of urea and guanidine hydrochloride (Gdn HCl) on solubilization of the polar, non-polar and peptide groups of horseradish peroxidase (HRP), an example of a globular protein, provide the driving force for unfolding of HRP, in a reversible two-state process. The intrinsic or conformational stability of HRP at various pH values and temperatures has been estimated by the linear extrapolation method (LEM), a denaturant binding model (DBM) and Tanford's model. There is good agreement between these methods. Tanford's model shows that urea interacts with non-polar groups to a greater extent than Gdn HCl does, whereas Gdn HCl interacts more effectively with the peptide groups of HRP.
Moosavi-Movahedi
A A
AA
Institute of Biochemistry and Biophysics, University of Tehran, Iran.
Nazari
K
K
D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D019791:Guanidine; D006146:Guanidines; D006735:Horseradish Peroxidase / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008956:Models, Chemical; D011489:Protein Denaturation; D013816:Thermodynamics; D014508:Urea
D006146:Guanidines; D046911:Macromolecular Substances; D014508:Urea; D006735:Horseradish Peroxidase; D019791:Guanidine