Complexities in the denaturation of horse metmyoglobin by guanidine hydrochloride.

F Ahmad

doi:10.1016/s0021-9258(19)85104-9

Abstract

The denaturation of horse metmyoglobin by guanidine hydrochloride was studied at pH 6.4 and 25 degrees C. Measurements of both the peptide circular dichroism and the absorbance in the Soret region suggest that the extent of renaturation strongly depends on the time interval during which the protein is exposed to concentrated solutions of the denaturant. From the equilibrium measurements of the absorption in the Soret region, it is concluded that the unfolding of metmyoglobin is complex. This is further supported by kinetic studies of denaturation which suggest the occurrence of the least four species in the reaction.

Highlights

Bismuto et al [2] analyzed their equilibrium results of GdnHCl denaturation of horse Mb in terms of a three-state process
It was reported thatthe GdnHCl denaturation is fully reversible and that thme echanism is close to a twoments at 25 “C were made in a Jasco-5OOA spectropolarimeter as described earlier [9]
A similar procedure wasemployed in preparing Mb solutions for renaturation experiments except that protein was first denatured in concentrated GdnHCl and thendiluted with the buffer

Summary

Introduction

Bismuto et al [2] analyzed their equilibrium results of GdnHCl denaturation of horse Mb in terms of a three-state process. A similar procedure wasemployed in preparing Mb solutions for renaturation experiments except that protein was first denatured in concentrated GdnHCl and thendiluted with the buffer.

Results

Conclusion