Open AccessA Dilatometric Study of the Denaturation of Lysozyme by Guanidine Hydrochloride and Hydrochloric Acid
Author(s) -
ŠKerjanc Jože,
Lapanje Savo
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb01665.x
Subject(s) - guanidine , hydrochloride , lysozyme , chemistry , hydrochloric acid , denaturation (fissile materials) , chromatography , nuclear chemistry , biochemistry , organic chemistry
The denaturation of lysozyme by guanidine hydrochloride and hydrochloric acid, and by guanidine hydrochloride alone at 25 °C was studied using a dilatometric technique. From results of the dilatometric measurements volume changes for partial and complete denaturation by hydrochloric acid at constant guanidine hydrochloride concentration were determined. The volume change due to unfolding per se in 3 M guanidine hydrochloride was found to be — 47 ml per mol of lysozyme. Volume changes were also determined for partial and complete denaturation of lysoyzme at 25 °C by guanidine hydrochloride alone at constant p H. The volume change due to unfolding per se in 6 M guanidine hydrochloride and p H 5.2 was determined to be — 54 ml per mol of lysozyme.