Determination of the number of binding sites and the mechanism of quenching about the bilirubin on human serum albumin by spectroscopic method

2011 ◽  
Vol 44 (13) ◽  
pp. S262
Author(s):  
Akram Hosenzadeh ◽  
Jamshid Chamani ◽  
Mohsen Gharanfoli
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Spectroscopic Method ◽  
Number Of Binding Sites

scholarly journals N-bromosuccinimide-oxidized human serum albumin as a tool for the determination of drug binding sites of human serum albumin.

1983 ◽  
Vol 31 (3) ◽  
pp. 971-978 ◽  
Author(s):  
HIROKO SAKAMOTO ◽  
IZUMI NAGATA ◽  
KIYOMI KIKUCHI ◽  
MASAKO AIDA ◽  
MASACHIKA IRIE
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Drug Binding Sites

scholarly journals Interaction of the Fungicide Tebuconazole with Human Serum Albumin: A Preliminary Study

2018 ◽  
Vol 62 (2) ◽  
pp. 85-91 ◽  
Author(s):  
J. Staničová ◽  
K. Želonková ◽  
V. Verebová ◽  
B. Holečková ◽  
J. Dianovský
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Triazole Fungicides ◽  
Number Of Binding Sites ◽  
Preliminary Study ◽  
Protein Macromolecule

Abstract The interactions between the fungicide tebuconazole and human serum albumin were investigated using fluorescence and circular dichroism spectroscopies. The experimental results showed that the fluorescence quenching of the protein by the tebuconazole molecule was a result of the formation of a ligand-protein complex with a binding constant of 8.51×103 l.mol−1 and the number of binding sites in the macromolecule was close to 1. These findings demonstrated the fact that although the binding affinity of tebuconazole to the protein may be slight, it was very similar to other triazole fungicides. In addition, tebuconazole stabilized the α-helical secondary structure of the human serum albumin due to the increase of the α-content in the protein macromolecule.

Spectroscopic and thermodynamic determination of three distinct binding sites for Co(II) ions in human serum albumin☆

2009 ◽  
Vol 103 (7) ◽  
pp. 1005-1013 ◽  
Author(s):  
Magdalena Sokołowska ◽  
Małgorzata Wszelaka-Rylik ◽  
Jarosław Poznański ◽  
Wojciech Bal
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Thermodynamic Determination

scholarly journals Simultaneous Determination of Human Serum Albumin and Low-Molecular-Weight Thiols after Derivatization with Monobromobimane

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3321
Author(s):  
Katarzyna Kurpet ◽  
Rafał Głowacki ◽  
Grażyna Chwatko
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Simultaneous Determination ◽  
Reversed Phase ◽  
Fluorescence Labeling ◽  
Detector Response ◽  
Low Molecular Weight

Biothiols are extremely powerful antioxidants that protect cells against the effects of oxidative stress. They are also considered relevant disease biomarkers, specifically risk factors for cardiovascular disease. In this paper, a new procedure for the simultaneous determination of human serum albumin and low-molecular-weight thiols in plasma is described. The method is based on the pre-column derivatization of analytes with a thiol-specific fluorescence labeling reagent, monobromobimane, followed by separation and quantification through reversed-phase high-performance liquid chromatography with fluorescence detection (excitation, 378 nm; emission, 492 nm). Prior to the derivatization step, the oxidized thiols are converted to their reduced forms by reductive cleavage with sodium borohydride. Linearity in the detector response for total thiols was observed in the following ranges: 1.76–30.0 mg mL−1 for human serum albumin, 0.29–5.0 nmol mL−1 for α-lipoic acid, 1.16–35 nmol mL−1 for glutathione, 9.83–450.0 nmol mL−1 for cysteine, 0.55–40.0 nmol mL−1 for homocysteine, 0.34–50.0 nmol mL−1 for N-acetyl-L-cysteine, and 1.45–45.0 nmol mL−1 for cysteinylglycine. Recovery values of 85.16–119.48% were recorded for all the analytes. The developed method is sensitive, repeatable, and linear within the expected ranges of total thiols. The devised procedure can be applied to plasma samples to monitor biochemical processes in various pathophysiological states.

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