Fluorescence study of nile red bound to human serum albumin in buffer, denaturant, and reverse micelles

1995 ◽  
Author(s):  
Daniel M. Davis ◽  
David J. S. Birch ◽  
P. R. Gellert ◽  
Rodney S. Kittlety ◽  
Ronald M. Swart
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Reverse Micelles ◽  
Nile Red ◽  
Fluorescence Study

Extrinsic fluorescence probe study of human serum albumin using Nile red

1996 ◽  
Vol 6 (1) ◽  
pp. 23-32 ◽  
Author(s):  
Daniel M. Davis ◽  
David J. S. Birch
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Probe ◽  
Nile Red

The fluorescence and circular dichroism of proteins in reverse micelles: application to the photophysics of human serum albumin and N-acetyl-l-tryptophanamide

1996 ◽  
Vol 60 (3) ◽  
pp. 63-77 ◽  
Author(s):  
Daniel M. Davis ◽  
David McLoskey ◽  
David J.S. Birch ◽  
Paul R. Gellert ◽  
Rodney S. Kittlety ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Reverse Micelles ◽  
Circular Dichroïsm

scholarly journals Fluorescence study on the interaction of human serum albumin with loureirin B

2010 ◽  
Vol 24 (5) ◽  
pp. 547-557 ◽  
Author(s):  
Xu Chen ◽  
Jia-Ming Ma ◽  
Ke-Lan Yong ◽  
Jing-Ci Lv ◽  
Xia-Bing Zhang
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Spectra ◽  
Three Dimensional ◽  
Entropy Change ◽  
Enthalpy Change ◽  
Dynamic Quenching ◽  
Fluorescence Study ◽  
Loureirin B

The interaction between loureirin B (Lour B) and human serum albumin (HSA) was investigated by fluorescence and UV–vis absorption spectroscopy. Experimental results indicated that loureirin B had a strong ability to quench the intrinsic fluorescence of HSA through a dynamic quenching procedure. The fluorescence quenching data revealed that the quenching constants (KSV) 2.68×104, 3.30×104and 4.10×104l/mol at 300, 310 and 320 K, respectively. Based on the thermodynamic parameters obtained, the positive values of enthalpy change ΔH and entropy change ΔS suggested that hydrophobic forces played a major role in the interaction of Lour B with HSA. According to Förster theory of energy transfer, the distancerbetween HSA and Lour B was calculated to be 2.85 nm. Furthermore, the effect of Lour B on the conformation of HSA was analyzed by synchronous fluorescence and three-dimensional fluorescence spectra.

Dynamics of Acrylodan-Labeled Bovine and Human Serum Albumin Sequestered within Aerosol-OT Reverse Micelles

1995 ◽  
Vol 67 (20) ◽  
pp. 3775-3781 ◽  
Author(s):  
Jeffrey S. Lundgren ◽  
Mark P. Heitz ◽  
Frank V. Bright
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Reverse Micelles ◽  
Aerosol Ot

scholarly journals Ligand binding at membrane mimetic interfaces. Human serum albumin in reverse micelles

1991 ◽  
Vol 199 (1) ◽  
pp. 79-87 ◽  
Author(s):  
Bernard DESFOSSES ◽  
Nicole CITTANOVA ◽  
Wladimir URBACH ◽  
Marcel WAKS
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Reverse Micelles ◽  
Membrane Mimetic

Fluorescence study on the interaction of human serum albumin with bromsulphalein

2006 ◽  
Vol 65 (5) ◽  
pp. 1144-1147 ◽  
Author(s):  
Fang-Qin Cheng ◽  
Ya-Ping Wang ◽  
Zhong-Ping Li ◽  
Chuan Dong
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Study
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