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Denaturation of Adenosine Deaminase with Urea and Guanidine Hydrochloride
Author(s) -
Moghaddamnia M. H.,
Saboury A. A.,
Hakimelahi G. H.,
MoosaviMoovahedi A. A.
Publication year - 1997
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.199700063
Subject(s) - chemistry , guanidine , denaturation (fissile materials) , urea , adenosine deaminase , hydrochloride , amp deaminase , molecule , chromatography , enzyme , biochemistry , nuclear chemistry , organic chemistry
The denaturation effect of urea and guanidine hydrochloride on (lie adenosine deaminase has been investigated spectrophotometrically at the two temperatures of 27 °C and 37 °C at pH = 7.50, phosphate buffer (55 mM). A simple, reversible two stale transition, N ⇔ D, was used to analyze the denaturation process from which conformational stability was estimated using three different methods, namely, the linear extrapolation method (LEM), Tanford's model (TM), and the denaturant binding method (DBM). A good agreement was observed among these methods. The results from free energy of denaturation at zero concentration of denaturant, ΔG° H2O , show the fragile conformation for adenosine deaminase molecule.