Aa. Moosavimovahedi et K. Nazari, DENATURATION OF HORSERADISH-PEROXIDASE WITH UREA AND GUANIDINE-HYDROCHLORIDE, International journal of biological macromolecules, 17(1), 1995, pp. 43-47
Favourable effects of urea and guanidine hydrochloride (Gdn HCl) on so
lubilization of the polar, non-polar and peptide groups of horseradish
peroxidase (HRP), an example of a globular protein, provide the drivi
ng 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 (LE
M), a denaturant binding model (DBM) and Tanford's model. There is goo
d agreement between these methods. Tanford's model shows that urea int
eracts with non-polar groups to a greater extent than Gdn HCl does, wh
ereas Gdn HCl interacts more effectively with the peptide groups of HR
P.