Resolution of ultrafast excited state kinetics of bilirubin in chloroform and bound to human serum albumin

2004 ◽  
Vol 6 (19) ◽  
pp. 4535 ◽  
Author(s):  
Burkhard Zietz ◽  
Alisdair N. Macpherson ◽  
Tomas Gillbro
Keyword(s):  
Excited State ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Kinetics Of

Polarographic studies on renaturation of urea-denatured human serum albumin

1989 ◽  
Vol 54 (2) ◽  
pp. 536-543 ◽  
Author(s):  
Josef Chmelík ◽  
Pavel Anzenbacher ◽  
Vítěz Kalous
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Irreversible Process ◽  
State Model ◽  
Native Protein ◽  
Main Components ◽  
Two State Model ◽  
Kinetics Of

The renaturation of the two main components of human serum albumin, i.e. of mercaptalbumin and nonmercaptalbumin, was studied polarographically. It has been demonstrated that renaturation of both proteins after 1-min denaturation in 8M urea is reversible. By contrast, renaturation after 200 min denaturation in 8M urea is an irreversible process; the characteristics of renatured mercaptalbumin differ more from the properties of the native protein than the characteristics of nonmercaptalbumin. The studies of the kinetics of renaturation of both proteins have shown that the renaturation can be represented by a two-state model. This means that the existence of stable intermediary products during the renaturation process was not determined polarographically.

Stereoselective kinetics of warfarin binding to human serum albumin: Effect of an allosteric interaction

Chirality ◽  
2002 ◽  
Vol 14 (5) ◽  
pp. 442-448 ◽  
Author(s):  
Ilona Fitos ◽  
J�lia Visy ◽  
Julianna Kardos
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Allosteric Interaction ◽  
Kinetics Of

Investigating the role of human serum albumin protein pocket on the excited state dynamics of indocyanine green using shaped femtosecond laser pulses

2015 ◽  
Vol 17 (8) ◽  
pp. 5872-5877 ◽  
Author(s):  
Muath Nairat ◽  
Arkaprabha Konar ◽  
Marie Kaniecki ◽  
Vadim V. Lozovoy ◽  
Marcos Dantus
Keyword(s):  
Excited State ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Indocyanine Green ◽  
Human Serum ◽  
Laser Pulses ◽  
Femtosecond Laser Pulses ◽  
Vibrational Motion ◽  
Protein Pocket

When indocyanine green (ICG) is confined inside the pocket of human serum albumin its triplet state formation is mitigated and coherent vibrational motion becomes more observable.

scholarly journals Effect of the binding of bilirubin to either the first class or the second class of binding sites of the human serum albumin molecule on its photochemical reaction

1989 ◽  
Vol 257 (3) ◽  
pp. 711-714 ◽  
Author(s):  
S Onishi ◽  
S Itoh ◽  
K Isobe ◽  
M Ochi ◽  
T Kunikata ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Serum Bilirubin ◽  
Bilirubin Concentration ◽  
Kinetics Of ◽  
Albumin Molecule ◽  
Human Serum Albumin Molecule ◽  
Serum Bilirubin Concentration

The kinetics of the photochemical changes of bilirubin were studied at a constant concentration of bilirubin bound either to the first class or to the second class of binding sites of the human serum albumin molecule. The more the bilirubin binds to the first class of binding sites in the human serum albumin molecule, the more readily geometric photoequilibrium to give (ZE)-bilirubin takes place. The more the bilirubin binds to the second class of binding sites or allosterically transformed binding sites induced by added SDS, the more readily structural photoisomerization, i.e. the formation of (EZ)-cyclobilirubin, takes place. When the serum bilirubin concentration is at low, safe, values bilirubin binds exclusively to the first class of binding sites and serves as an antioxidant [Onishi, Yamakawa & Ogawa (1971) Perinatology 1, 373-379]; at these concentrations human serum albumin protects bilirubin from irreversible photodegradation by only allowing readily reversible geometric photoisomerization. As the serum bilirubin concentration increases to high, and potentially dangerous, values, bilirubin binds to the second class of binding sites, and under these conditions human serum albumin seems to promote the photocyclization of bilirubin. During irradiation human serum albumin seems to act by retaining low, useful, concentrations of bilirubin while facilitating irreversible photoisomerization of excess bilirubin.

Human serum albumin (HSA) nanoparticles: Reproducibility of preparation process and kinetics of enzymatic degradation

2008 ◽  
Vol 347 (1-2) ◽  
pp. 109-117 ◽  
Author(s):  
K. Langer ◽  
M.G. Anhorn ◽  
I. Steinhauser ◽  
S. Dreis ◽  
D. Celebi ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Enzymatic Degradation ◽  
Preparation Process ◽  
Kinetics Of

Kinetics of Interaction of Local Anesthetics with Human Serum Albumin

2005 ◽  
Vol 140 (3) ◽  
pp. 315-316 ◽  
Author(s):  
A. P. Galenko-Yaroshevskii ◽  
P. N. Fistunenko ◽  
A. S. Dukhanin
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Local Anesthetics ◽  
Kinetics Of
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