scholarly journals Kinetics of Peroxynitrite Reaction with Amino Acids and Human Serum Albumin

1999 ◽  
Vol 274 (2) ◽  
pp. 842-848 ◽  
Author(s):  
Beatriz Alvarez ◽  
Gerardo Ferrer-Sueta ◽  
Bruce A. Freeman ◽  
Rafael Radi
Keyword(s):  
Amino Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Kinetics Of

Kinetics of peroxynitrite reaction with amino acids and human serum albumin

1998 ◽  
Vol 25 ◽  
pp. S65
Author(s):  
Rafael Radi ◽  
Beatriz Alvarez ◽  
Gerardo Ferrer-Sueta ◽  
Bruce A. Freeman
Keyword(s):  
Amino Acids ◽  
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

In vitro stereoselective degradation of carprofen glucuronide by human serum albumin. Characterization of sites and reactive amino acids

Chirality ◽  
2000 ◽  
Vol 12 (2) ◽  
pp. 53-62 ◽  
Author(s):  
H�l�ne Georges ◽  
Nathalie Presle ◽  
Thierry Buronfosse ◽  
Sylvie Fournel-Gigleux ◽  
Patrick Netter ◽  
...  
Keyword(s):  
Amino Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Stereoselective Degradation

Exploring the Molecular Level Interaction of Human Serum Albumin with Calcium Oxalate Monohydrate Crystals

2021 ◽  
Vol 28 ◽  
Author(s):  
Priyadarshini ◽  
Abhishek Negi ◽  
Chetna Faujdar ◽  
Lokesh Nigam ◽  
Naidu Subbarao
Keyword(s):  
Amino Acids ◽  
Crystal Growth ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Calcium Oxalate ◽  
Human Serum ◽  
Stone Formation ◽  
Calcium Oxalate Monohydrate ◽  
Calcium Oxalate Crystallization ◽  
In Silico Docking

Background: Human serum albumin (HSA) is one of the most abundant proteins in the blood plasma, urine as well as in the organic matrix of renal calculi. Macromolecules present in the urine modulate kidney stone formation either by stimulating or inhibiting crystallization process. Objective: In the present study, effect of HSA protein on the growth of calcium oxalate monohydrate crystal (COM) was investigated. Methods: Crystal growth assay was used to measure oxalate depletion in the crystal seeded solution in the presence of HSA. HSA concentrations exhibiting effect on crystal growth were selected for FTIR and XRD analysis. In silico docking was performed on seven different binding sites of HSA. Results: Albumin is playing dual role in growth of calcium oxalate crystallization. FTIR and XRD studies further revealed HSA exerted strain over crystal thus affecting its structure by interacting with amino acids of its pocket 1. Docking results indicate that out of 7 binding pocket in protein, calcium oxalate interacts with Arg-186 and Lys-190 amino acids of pocket 1. Conclusion: Our study confirms the role of HSA in calcium oxalate crystallization where acidic amino acids arginine and lysine are binding with COM crystals, revealing molecular interaction of macromolecule and crystal in urolithiasis.

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