- 作者: 崔鳳靈, 王俊麗, 崔延瑞, 李建平
- 作者服務機構: School of Chemistry and Environmental Science, Key Laboratory for Environmental Pollution Control Technology of Henan Province, Henan Normal University, Xinxiang 453007, P. R. China
- 中文摘要: Under physiological conditions, interaction between N,N¢-di(4-chlorophenyl)thiourea synthesized and human serum albumin was investigated by using fluorescence spectroscopy and UV absorption spectrum. The intrinsic fluorescence of human serum albumin was quenched by N,N¢-di(4-chlorophenyl)-thiourea through a static quenching procedure. The binding constants (K) at 14 °C and 24 °C were obtained, and the values were 2.541 ’ 105 M-1 and 2.021 ’ 105 M-1, respectively. Thermodynamic parameter enthalpy change (DH) and entropy change (DS) were calculated to be -16.19 KJ/mol and 47.05 J·mol-1·K-1, respectively, which indicated that hydrophobic force played a major role in interaction. The binding distance was evaluated on the basis of the theory of Foster energy transfer. The effects of various metal ions on the binding constants of N,N¢-di(4-chlorophenyl)thiourea with human serum albumin were studied. A synchronous fluorescence technique for determination of human serum albumin was developed, and the method was successfully applied to the detection of HSA in human serum samples.
- 英文摘要: --
- 中文關鍵字: N,N¢-di(4-chlorophenyl)thiourea (DCPT); Human serum albumin (HSA); Synchronous fluorescence; Determination.
- 英文關鍵字: --