Influence of complex formation with tetraantraquinoporphyrazines and tetrasulphophthalocyanine on thermal stability of bovine serum albumin

2011 ◽  
Vol 15 (04) ◽  
pp. 223-229 ◽  
Author(s):  
Natalia Lebedeva ◽  
Tatyana Popova ◽  
Malgorzata Kozbial ◽  
Malgorzata Wszelaka-Rylik ◽  
Yuri Gubarev ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Differential Scanning Calorimetry ◽  
Bovine Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Denaturation ◽  
Scanning Calorimetry ◽  
Electron Absorption Spectroscopy ◽  
Thermal Stability Of

Interaction between bovine serum albumin (BSA) and tetraantraquinoporphyrazines (TAP) and tetrasulphophthalocyanine (Pc) aluminum hydroxide was studied by means of electron absorption spectroscopy, IR spectroscopy, fluorescence spectroscopy and differential scanning calorimetry. It was found that the complex formation of BSA with the TAPs results in increase of thermal stability of the protein while Pc does not have remarkable influence on the protein thermal denaturation.

A novel amalgamation of deep eutectic solvents and crowders as biocompatible solvent media for enhanced structural and thermal stability of bovine serum albumin

2020 ◽  
Vol 22 (42) ◽  
pp. 24410-24422
Author(s):  
Kavya Bhakuni ◽  
Niketa Yadav ◽  
Pannuru Venkatesu
Keyword(s):  
Thermal Stability ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Deep Eutectic Solvents ◽  
Solvent Medium ◽  
Thermal Stability Of

This study unravels the effect of a novel solvent medium designed by amalgamation of macromolecular crowders and deep eutectic solvents (DESs) on bovine serum albumin (BSA).

Heteroprotein complex formation of bovine serum albumin and lysozyme: Structure and thermal stability

2018 ◽  
Vol 74 ◽  
pp. 267-274 ◽  
Author(s):  
Monique Barreto Santos ◽  
Carlos Wanderlei Piler de Carvalho ◽  
Edwin Elard Garcia-Rojas
Keyword(s):  
Thermal Stability ◽  
Bovine Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Bovine Serum

scholarly journals A DSC study of zinc binding to bovine serum albumin (BSA)

2007 ◽  
Vol 72 (4) ◽  
pp. 331-337 ◽  
Author(s):  
Sanja Ostojic ◽  
Vida Dragutinovic ◽  
Miodrag Kicanovic ◽  
Branislav Simonovic
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Denaturation ◽  
Protein Unfolding ◽  
Protein Denaturation ◽  
Binding Constants ◽  
Zinc Binding ◽  
Scanning Calorimetry ◽  
The Stability

The thermal denaturation of bovine serum albumin (BSA) is a kinetically and thermodynamically controlled process. The effects of zinc binding to bovine serum albumin (BSA), followed by differential scanning calorimetry (DSC), were investigated in this work, with the purpose of obtaining a better understanding of the albumin/zinc interaction. From the DSC curves, the thermodynamic parameters of protein denaturation were obtained, i.e., the temperature of thermal transition maximum (T m), calorimetric enthalpy (?Hcal), van't Hoff enthalpy (?HvH), the number of binding sites (I, II), the binding constants for each binding site (K bI, K bII) and the average number of ligands bound per mole of native protein X N. The thermodynamic data of protein unfolding showed that zinc binding to bovine serum albumin increases the stability of the protein (higher values of ?Hcal) and the different ratio ?Hcal/?HvH indicates the perturbation of the protein during thermal denaturation.

Interactions Analysis in BSA-Loaded Chitosan Nanoparticles at Different pH Values

2011 ◽  
Vol 694 ◽  
pp. 160-164 ◽  
Author(s):  
Yong Liu ◽  
Yan Sun ◽  
Yan Li Li ◽  
Shao Chun Xu ◽  
Yao Xing Xu
Keyword(s):  
Differential Scanning Calorimetry ◽  
Fourier Transform ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sodium Tripolyphosphate ◽  
Chitosan Nanoparticles ◽  
Scanning Calorimetry ◽  
Ph Values ◽  
Protein Bovine Serum Albumin

In this paper, the properties of chitosan nanoparticles and bovine serum albumin-loaded chitosan nanoparticles prepared with sodium tripolyphosphate at different pH values were discussed. Interactions in chitosan nanoparticles and bovine serum albumin-loaded chitosan nanoparticles were analyzed by Fourier transform infrared spectroscopy and differential scanning calorimetry. The results indicated that there were more complicated interactions in chitosan nanoparticles prepared at different pH values. When the pH values were lower or higher than isoelectric point value of target protein (bovine serum albumin), the big different interactions occurred in chitosan nanoparticles. These differences also would result in different releasing properties.

Buffers more than buffering agent: introducing a new class of stabilizers for the protein BSA

2015 ◽  
Vol 17 (2) ◽  
pp. 1114-1133 ◽  
Author(s):  
Bhupender S. Gupta ◽  
Mohamed Taha ◽  
Ming-Jer Lee
Keyword(s):  
Thermal Stability ◽  
Light Scattering ◽  
Bovine Serum Albumin ◽  
Dynamic Light Scattering ◽  
Serum Albumin ◽  
Bovine Serum ◽  
New Class ◽  
Buffering Agent ◽  
Thermal Stability Of ◽  
Biological Buffers

In this study, we have analyzed the influence of four biological buffers on the thermal stability of bovine serum albumin (BSA) using dynamic light scattering (DLS).

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