Molybdenum-95 n.m.r. spectroscopy as a probe of biological systems: the detection of tetraoxo- and tetrathio-molybdate(VI) bound to bovine serum albumin

1985 ◽  
pp. 479 ◽  
Author(s):  
Stuart Bristow ◽  
C. David Garner ◽  
Stuart K. Hagyard ◽  
Gareth A. Morris ◽  
John R. Nicholson ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Biological Systems

Surface chemistry of bovine serum albumin with hematite nanoparticles and its effect on arsenate adsorption

2021 ◽  
Vol 18 (4) ◽  
pp. 177
Author(s):  
A. M. Eid ◽  
Shea Kraemer ◽  
Hind A. Al-Abadleh
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Chemistry ◽  
Adsorption Kinetics ◽  
Bovine Serum ◽  
Active Sites ◽  
Binding Free Energy ◽  
Biological Systems ◽  
Hematite Nanoparticles ◽  
Arsenate Adsorption

Environmental contextHematite nanoparticles are efficient adsorbents for proteins and pollutants in environmental and biological systems. Hematite and the protein bovine serum albumin (BSA) were used as models to investigate the surface chemistry and competitive role of BSA in arsenate adsorption. Results show that surface BSA inhibits arsenate adsorption, potentially altering its mobility and bioavailability. AbstractThe surface chemistry of metal oxide nanomaterials controls their health impacts and fate in environmental and biological systems. These systems contain proteins capable of binding to nanoparticles, which forms a protein corona that modifies the surface properties of the nanoparticles and reactivity towards pollutants. Using attenuated total reflectance-Fourier transform infrared (ATR-FTIR) spectroscopy, we investigate the adsorption of bovine serum albumin (BSA) and quantify the competitive effect of BSA on the adsorption kinetics of arsenate, AsV, to hematite nanoparticles. Experiments were conducted in the flow mode at pH 7. BSA was first adsorbed on hematite, then AsV was allowed to flow over the BSA/hematite thin film. Adsorption kinetic and thermodynamic parameters were calculated using a modified Langmuir adsorption model for both BSA and AsV. The adsorption thermodynamic model showed that BSA binds through two active sites with a binding energy of –41 kJ mol−1, which corresponds to the spontaneous formation of chemisorbed and physisorbed species. When AsV flowed over the BSA/hematite film, only 11 % of surface BSA was desorbed by AsV. This result highlights the inhibitory effect of BSA for AsV adsorption. Structural analysis of BSA revealed changes to the local conformational geometry upon adsorption to and desorption from hematite nanoparticles. Molecular docking simulations showed that the binding free energy of a modelled hematite nanoparticle towards the BSA surface is –6.8 kcal mol−1 (−28.5 kJ mol−1) owing to the formation of various bonds, which agrees with the adsorption kinetics modelling. Overall, surface BSA inhibits arsenate adsorption and therefore increases its mobility and bioavailability.

scholarly journals Surface-enhanced Raman scattering investigation of bovine serum albumin by Au nanoparticles with different sizes

2018 ◽  
Vol 16 (1_suppl) ◽  
pp. 157-162 ◽  
Author(s):  
Wei Xiaodan ◽  
Zheng Dawei ◽  
Zhang Ping ◽  
Lin Taifeng ◽  
Wang Huiqin ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Raman Scattering ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Au Nanoparticles ◽  
Structural Information ◽  
Biological Systems ◽  
Surface Enhanced ◽  
Surface Enhanced Raman ◽  
Enhanced Raman Scattering

Background: Surface-enhanced Raman scattering (SERS) has become a useful spectroscopic tool for studying biomolecule structures. The main types of plasmonic substrates used in biological systems are Au nanoparticles (AuNPs), whose surface plasmon resonance depends on the nanoparticle size, morphology, particle interspace, and so on. Methods: In this study, AuNP colloids with different sizes were synthesized and used as the sensors to probe SERS signals of different biomarkers and biomolecules. Results: The results showed that an AuNP colloid of ~50 nm had excellent SERS effects in probing various molecules, and could be preserved for about 3 months with excellent repeatability and reproducibility (RSD <5%) in terms of the probed signal intensity (rhodamine 6G and crystal violet). Meanwhile, the fabricated AuNPs were applied to study the SERS signals and structural information of bovine serum albumin (BSA) in aqueous solution. It was found that SERS could rapidly provide the structural information and vibration characteristics of BSA. Conclusion: It was concluded that biocompatible AuNP colloid may be a promising biosensor in the rapid and label-free detection of biological systems.

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.

RADIOIMMUNOASSAY OF OESTRONE AND OESTRADIOL IN THE PERIPHERAL PLASMA OF THE DOMESTIC FOWL IN VARIOUS PHYSIOLOGICAL STATES AND OF HYPOPHYSECTOMIZED AND OVARIECTOMIZED FOWLS

1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Diethyl Ether ◽  
Bovine Serum ◽  
Domestic Fowl ◽  
Laying Hens ◽  
Peripheral Plasma ◽  
The Mean ◽  
Precision And Accuracy ◽  
Chicken Ovary

ABSTRACT A radioimmunoassay was developed to measure the levels of oestrone and oestradiol in 0.5–1.0 ml of domestic fowl peripheral plasma. The oestrogens were extracted with diethyl ether, chromatographed on columns of Sephadex LH-20 and assayed with an antiserum prepared against oestradiol-17β-succinyl-bovine serum albumin using a 17 h incubation at 4°C. The specificity, sensitivity, precision and accuracy of the assays were satisfactory. Oestrogen concentrations were determined in the plasma of birds in various reproductive states. In laying hens the ranges of oestrone and oestradiol were 12–190 pg/ml and 29–327 pg/ml respectively. Levels in immature birds, in adult cockerels and in an ovariectomized hen were barely detectable. The mean concentrations of oestrone and oestradiol in the plasma of four non-laying hens (55 pg/ml and 72 pg/ml respectively) and one partially ovariectomized hen (71 pg/ml and 134 pg/ml respectively) were well within the range for laying hens. It is evident that the large, yolk-filled follicles are not the only source of oestrogens in the chicken ovary.

Interaction of 1,4,7,10-Tetraazacyclododecane-Co(Ⅱ) with Bovine Serum Albumin

2013 ◽  
Vol 30 (2) ◽  
pp. 232
Author(s):  
Fan LIU ◽  
Yuanqin ZHANG ◽  
Zhijin ZHANG
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum
Sign in / Sign up

Export Citation Format

Share Document