Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy

2009 ◽  
Vol 147 (2) ◽  
pp. 191-200 ◽  
Author(s):  
T. Otosu ◽  
E. Nishimoto ◽  
S. Yamashita
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational State ◽  
Tryptophan Residue ◽  
Time Resolved Fluorescence ◽  
Time Resolved

Interaction of human serum albumin with liposomes of saturated and unsaturated lipids with different phase transition temperatures: a spectroscopic investigation by membrane probe PRODAN

RSC Advances ◽  
2014 ◽  
Vol 4 (28) ◽  
pp. 14335-14347 ◽  
Author(s):  
Raina Thakur ◽  
Anupam Das ◽  
Anjan Chakraborty
Keyword(s):  
Phase Transition ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Techniques ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Unsaturated Lipids ◽  
Membrane Probe ◽  
Phase Transition Temperatures

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.

scholarly journals Interaction of Cm(III) with human serum albumin studied by time-resolved laser fluorescence spectroscopy and NMR

2019 ◽  
Vol 192 ◽  
pp. 45-51
Author(s):  
Nicole Adam ◽  
Christian Adam ◽  
Markus Keskitalo ◽  
Jonathan Pfeuffer-Rooschüz ◽  
Petra J. Panak
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Laser Fluorescence ◽  
Time Resolved ◽  
Laser Fluorescence Spectroscopy

Time-resolved fluorescence studies on site-directed mutants of human serum albumin

FEBS Letters ◽  
1997 ◽  
Vol 408 (1) ◽  
pp. 67-70 ◽  
Author(s):  
Michael K Helms ◽  
Charles E Petersen ◽  
Nadhipuram V Bhagavan ◽  
David M Jameson
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Fluorescence Studies

Binding interaction and conformational changes of human serum albumin with ranitidine studied by spectroscopic and time-resolved fluorescence methods

2016 ◽  
Vol 13 (7) ◽  
pp. 1325-1338 ◽  
Author(s):  
Manjunath D. Meti ◽  
Sharanappa T. Nandibewoor ◽  
Shrinivas D. Joshi ◽  
Uttam A. More ◽  
Shivamurti A. Chimatadar
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Time Resolved Fluorescence ◽  
Binding Interaction ◽  
Time Resolved ◽  
Fluorescence Methods

scholarly journals Unfolding of Acrylodan-Labeled Human Serum Albumin Probed by Steady-State and Time-Resolved Fluorescence Methods

1998 ◽  
Vol 75 (2) ◽  
pp. 1084-1096 ◽  
Author(s):  
Kulwinder Flora ◽  
John D. Brennan ◽  
Gary A. Baker ◽  
Meagan A. Doody ◽  
Frank V. Bright
Keyword(s):  
Steady State ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Fluorescence Methods

Glycation of Human Serum Albumin by DL-Glyceraldehyde: A Fluorescence Quenching Study

1997 ◽  
Vol 62 (11) ◽  
pp. 1815-1820 ◽  
Author(s):  
Miroslav Štěpánek ◽  
Zdeněk Pavlíček
Keyword(s):  
Steady State ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Decay ◽  
Fluorescence Lifetimes ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Trp Fluorescence ◽  
Quenching Efficiency

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.

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