Steady State and Time-resolved Fluorescence Investigation of the Specific Binding of Two Chlorin Derivatives with Human Serum Albumin

2007 ◽  
Vol 111 (35) ◽  
pp. 10557-10562 ◽  
Author(s):  
Sunita Patel ◽  
Anindya Datta
1998 ◽  
Vol 75 (2) ◽  
pp. 1084-1096 ◽  
Author(s):  
Kulwinder Flora ◽  
John D. Brennan ◽  
Gary A. Baker ◽  
Meagan A. Doody ◽  
Frank V. Bright

1997 ◽  
Vol 62 (11) ◽  
pp. 1815-1820 ◽  
Author(s):  
Miroslav Štěpánek ◽  
Zdeněk Pavlíček

Process of glycation of human serum albumin (HSA) by DL-glyceraldehyde was studied using steady-state and time-resolved fluorescence spectroscopy in the course of 100 h. During this period, measurements of steady-state tryptophan (Trp) and non-tryptophan (non-Trp) fluorescence of the glycated HSA were carried out, together with measurement of the non-Trp fluorescence decay and steady-state quenching using potassium iodide as a quencher. Observed changes in both Trp and non-Trp fluorescence intensity, as well as changes in non-Trp fluorescence lifetimes and quenching efficiency are explained with respect to a probable mechanism of glycation.


RSC Advances ◽  
2014 ◽  
Vol 4 (28) ◽  
pp. 14335-14347 ◽  
Author(s):  
Raina Thakur ◽  
Anupam Das ◽  
Anjan Chakraborty

The interaction of human serum albumin (HSA) with liposomes made of saturated and unsaturated phosphocholines has been studied using circular dichroism (CD), steady state and time resolved fluorescence spectroscopic techniques.


FEBS Letters ◽  
1997 ◽  
Vol 408 (1) ◽  
pp. 67-70 ◽  
Author(s):  
Michael K Helms ◽  
Charles E Petersen ◽  
Nadhipuram V Bhagavan ◽  
David M Jameson

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