Study on the interaction between bovine serum albumin and inhalation anesthetic halothane by differential scanning calorimetry

2005 ◽  
Vol 1283 ◽  
pp. 326-327 ◽  
Author(s):  
Makoto Nishimoto ◽  
Hitoshi Matsuki ◽  
Shoji Kaneshina ◽  
Kenji Ogli
Keyword(s):  
Differential Scanning Calorimetry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Scanning Calorimetry ◽  
Inhalation Anesthetic

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.

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.

Effect of an inhalation anesthetic on the viscosity of aqueous bovine serum albumin solutions

2005 ◽  
Vol 1283 ◽  
pp. 322-323 ◽  
Author(s):  
Ukyo Komatsu ◽  
Hitoshi Matsuki ◽  
Shoji Kaneshina ◽  
Kenji Ogli
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Inhalation Anesthetic

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.

scholarly journals Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

Molecules ◽  
2021 ◽  
Vol 26 (21) ◽  
pp. 6565
Author(s):  
Ola Grabowska ◽  
Małgorzata M. Kogut ◽  
Krzysztof Żamojć ◽  
Sergey A. Samsonov ◽  
Joanna Makowska ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Titration Calorimetry ◽  
Scanning Calorimetry ◽  
Experimental Conditions ◽  
Potential Binding ◽  
Cacodylate Buffer ◽  
Helical Content

The binding interactions of bovine serum albumin (BSA) with tetraphenylborate ions ([B(Ph)4]−) have been investigated by a set of experimental methods (isothermal titration calorimetry, steady-state fluorescence spectroscopy, differential scanning calorimetry and circular dichroism spectroscopy) and molecular dynamics-based computational approaches. Two sets of structurally distinctive binding sites in BSA were found under the experimental conditions (10 mM cacodylate buffer, pH 7, 298.15 K). The obtained results, supported by the competitive interactions experiments of SDS with [B(Ph)4]− for BSA, enabled us to find the potential binding sites in BSA. The first site is located in the subdomain I A of the protein and binds two [B(Ph)4]− ions (logK(ITC)1 = 7.09 ± 0.10; ΔG(ITC)1 = −9.67 ± 0.14 kcal mol−1; ΔH(ITC)1 = −3.14 ± 0.12 kcal mol−1; TΔS(ITC)1 = −6.53 kcal mol−1), whereas the second site is localized in the subdomain III A and binds five ions (logK(ITC)2 = 5.39 ± 0.06; ΔG(ITC)2 = −7.35 ± 0.09 kcal mol−1; ΔH(ITC)2 = 4.00 ± 0.14 kcal mol−1; TΔS(ITC)2 = 11.3 kcal mol−1). The formation of the {[B(Ph)4]−}–BSA complex results in an increase in the thermal stability of the alfa-helical content, correlating with the saturation of the particular BSA binding sites, thus hindering its thermal unfolding.

scholarly journals PENGEMBANGAN SISTEM PEMBAWA ALBUMIN NANOPARTIKEL UNTUK SILIMARIN DAN KAJIAN SIFAT FISIK SERTA PROFIL PELEPASANNYA SECARA IN VITRO

2017 ◽  
Vol 7 (2) ◽  
pp. 23-29
Author(s):  
Rini Ambarwati ◽  
Heni Rachmawati
Keyword(s):  
Differential Scanning Calorimetry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Loading Capacity ◽  
X Ray Diffraction ◽  
Silybum Marianum ◽  
Scanning Calorimetry ◽  
X Ray

Silimarin merupakan senyawa flavonolignan yang berasal dari tumbuhan Silybum marianum (Asteraceae). Silimarin memiliki efek farmakologi sebagai antikanker dan hepatoprotektor, tetapi senyawa ini memiliki kelarutan yang rendah dalam air. Tujuan penelitian ini adalah mengembangkan formulasi silimarin dalam sistem pembawa nano dengan teknik desolvasi. Pembawa yang digunakan adalah serum albumin (bovine serum albumin/BSA). Kombinasi silimarin dalam BSA diharapkan dapat meningkatkan efikasi silimarin sebagai anti kanker karena permeabilitas BSA yang lebih baik pada sel kanker. Evaluasi standar terhadap nanopartikel silimarin-BSA meliputi ukuran dan distribusi ukuran partikel, zeta potensial, morfologi nanopartikel, kristalinitas, sifat termal, spektroskopi inframerah, efisiensi penjeratan serta profil pelepasan silimarin dari BSA nanopartikel pada 2 media berbeda (HCl 0,1 N & PBS pH 7,4). Nanopartikel BSA- silimarin memiliki ukuran partikel 174,23 13,94 nm; distribusi ukuran partikel 0,185 0,052; efisiensi penjeratan 90,54 0,098 %; loading capacity 30,18 0,036 % dan zeta potensial -1,62 mV. Hasil analisis menggunakan DSC (differential scanning calorimetry), XRD (X-ray diffraction) dan spektroskopi inframerah menunjukan bahwa nanopartikel silimarin berhasil terenkapsulasi di dalam nanopartikel BSA, dan BSA-silimarin memiliki bentuk amorf. Setelah 1 jam uji pelepasan, terdapat sebanyak 21,89% silimarin terlepas dalam HCl 0,1 N dan 54,84% silimarin terlepas dalam PBS pH 7,4 sehingga dapat disimpulkan bahwa silimarin-BSA memiliki kelarutan yang baik dalam air. Oleh karena itu, perlu dilakukan pengujian lebih lanjut untuk mengkaji akt ivitas serta perilaku silimarin-BSA in vivo untuk mengkonfirmasi data in vitro.

scholarly journals Effects of formaldehyde fixation on protein secondary structure: a calorimetric and infrared spectroscopic investigation.

1991 ◽  
Vol 39 (2) ◽  
pp. 225-229 ◽  
Author(s):  
J T Mason ◽  
T J O'Leary
Keyword(s):  
Secondary Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Secondary Structure ◽  
High Sensitivity ◽  
Ribonuclease A ◽  
Scanning Calorimetry ◽  
Temperature Range ◽  
Protein Molecules

We investigated the effects of formaldehyde fixation on the secondary structure of isolated proteins (bovine serum albumin, ribonuclease A, and hemoglobin) using high-sensitivity differential scanning calorimetry and Fourier transform infrared spectroscopy. Whereas thermograms obtained by scanning calorimetry on unfixed purified proteins demonstrated denaturation transitions in the 70-90 degrees C temperature range, the thermograms showed no denaturation transitions in this temperature range when the proteins had been placed in formaldehyde solutions. Thus, fixation destroyed the denaturation transition of bovine serum albumin, ribonuclease A, and hemoglobin. Infrared spectra obtained on the unfixed and fixed proteins were essentially identical. This demonstrates that the "fixed" proteins retain the secondary structure present before fixation. We therefore conclude that the cross-linking of proteins that occurs in the process of formaldehyde fixation "locks in" the secondary structure of these protein molecules.

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

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