Structure-affinity relationship of bovine serum albumin with dietary flavonoids with different C-ring substituents in the presence of Fe3+ ion

Interaction between dietary flavonoids and albumins plays an important role in the bioavailability and bioactivity of flavonoids. Therefore, the influence of this interaction on the antioxidant activity of flavonoid has attracted much interest. In this study, a ceric reducing/antioxidant capacity assay (CRAC) was employed to investigate the effects of albumin-flavonoid interaction on the antioxidant activity of seven common flavonoids. The results obtained from the CRAC assay were also compared separately with the results from the spectrophotometric methods including 2,2-diphenyl-1-picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) assays. All the flavonoids show a decreasing in the antioxidant activity detected by CRAC assay, indicting a “masking effect” of bovine serum albumin (BSA)-flavonoid interaction. However, the results from DPPH and FRAP assays were conflicting, which may be attributed to the influence of solvent systems.

Download Full-text

A mutispectroscopic study on the structure–affinity relationship of the interactions of bisphenol analogues with bovine serum albumin

Chemosphere ◽

10.1016/j.chemosphere.2021.132769 ◽

2021 ◽

pp. 132769

Author(s):

Jiali Gu ◽

Xiyao Huang ◽

Hongrui Liu ◽

Dianbo Dong ◽

Xuekai Sun

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Bisphenol Analogues ◽

Relationship Of

Download Full-text

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

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100128122 ◽

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.

Download Full-text

The adsorption of bovine serum albumin at the stainless-steel/aqueous solution interface

Journal of Colloid and Interface Science ◽

10.1016/s0021-9797(84)80018-1 ◽

1984 ◽

Vol 98 (1) ◽

pp. 138-143 ◽

Cited By ~ 4

Author(s):

H VANENCKEVORT ◽

D DASS ◽

A LANGDON

Keyword(s):

Aqueous Solution ◽

Stainless Steel ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Solution Interface

Download Full-text

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

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653438 ◽

1981 ◽

Vol 46 (03) ◽

pp. 645-647 ◽

Cited By ~ 28

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.

Download Full-text