- 作者: Moghaddamnia, M.H. ; Saboury, A.A. ; Hakimelahi, G.H. et al.
- 作者服務機構: Inst. of Biochemistry and Biophysics, Univ. of Tehran, Tehraran, Iran
- 中文摘要: The denaturation effect of urea and guanidine hydrochloride on the adenosine deaminase has been investigated spectrophotometrically at the two temperatures of 27.degree.C and 37.degree.C at pH=7.50, phosphate buffer(55mM). A simple, reversible two state transition, N.darrlr.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,.DELTA.G.degree./sub H2O/, show the fragile conformation for adenosine deaminase molecule.
- 英文摘要: --
- 中文關鍵字: Adenosine Deaminase; Denaturation; Urea; Guanidine Hydrochloride; Conformational Stability
- 英文關鍵字: 腺□脫氨;變性;尿素;胍氯化氫;構形穩定性