Quantitative investigation of the dynamic interaction of human serum albumin with procaine using a multi-way calibration method coupled with three-dimensional fluorescence spectroscopy

2015 ◽  
Vol 7 (16) ◽  
pp. 6552-6560 ◽  
Author(s):  
Li-Xia Xie ◽  
Hai-Long Wu ◽  
Chao Kang ◽  
Shou-Xia Xiang ◽  
Xiao-Li Yin ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Three Dimensional ◽  
Interaction Mechanism ◽  
Calibration Method ◽  
Dynamic Interaction ◽  
Effect Of Temperature ◽  
Quantitative Investigation

Based on a multi-way calibration method, free human serum albumin in a dynamic interaction system with procaine is quantified. Their interaction mechanism and the effect of temperature on interaction are also studied.

Effect of Temperature and Solvent on Fibrillation of Human Serum Albumin

2015 ◽  
Vol 22 (2) ◽  
pp. 112-118 ◽  
Author(s):  
Nitin Pandey ◽  
Sudeshna Ghosh ◽  
Debi Tripathy ◽  
Swagata Dasgupta
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Effect Of Temperature

scholarly journals Interaction between Alizarin and Human Serum Albumin by Fluorescence Spectroscopy

2011 ◽  
Vol 27 (1) ◽  
pp. 79-84 ◽  
Author(s):  
Feng GE ◽  
Lixiang JIANG ◽  
Diqiu LIU ◽  
Chaoyin CHEN
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum

scholarly journals Three-dimensional structure of human serum albumin

Science ◽  
1989 ◽  
Vol 244 (4909) ◽  
pp. 1195-1198 ◽  
Author(s):  
D. Carter ◽  
X. He ◽  
S. Munson ◽  
P. Twigg ◽  
K. Gernert ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

FLUORESCENCE CHANGE OF HUMAN SERUM ALBUMIN INDUCED BY METHYL VIOLET

2020 ◽  
Vol 54 (3 (253)) ◽  
pp. 261-264
Author(s):  
M.A. Shahinyan ◽  
N.H. Petrosyan ◽  
A.P. Antonyan
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Change ◽  
Fluorescence Intensity ◽  
Methyl Violet ◽  
Spectroscopy Method ◽  
Intensity Maximum ◽  
Fluorescence Change

The interaction of methyl violet (MV) with human serum albumin (HSA) has been studied, using the fluorescence spectroscopy method. It was shown that MV chnages the own fluorescence of HSA. It was also shown that MV does not induce any conformational change in the structure of HSA, since there is no change of the wavelength of HSA fluorescence intensity maximum. MV binds to HSA, near to fluorescing tryptophan, which in the hydrophilic environment, and changes the own fluorescence of the protein.

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