1. Data show that the fluorescence quenching process may occur through energy transfer from singlet excited state of tryptophan in BSA to the corresponding level of ASP. PMID: 20667434
2. Data indicate that CD spectroscopy of the HSA and BSA released in solution after desorption from the matrices shows that, while both proteins partially regain their helical structure, they show a distinct behaviour in their tertiary structure. PMID: 20692819
3. new insights on bovine serum albumin self-assembly process PMID: 21303653
4. Glass transition and dynamics in BSA-water mixtures over wide ranges of composition studied by thermal and dielectric techniques. PMID: 21798376
5. The results indicated that the binding abilities of vitamin B12 to BSA in the acidic and basic pH regions (pH 2.5, 3.5, 5.0, and 9.0) were lower than that at simulating physiological condition (pH 7.4). PMID: 21955947
6. The unfolding and refolding of BSA appear to proceed through intermediates and both the processes are sequential in nature. PMID: 21993230
7. The results showed that the riboflavin could efficiently bind to BSA in aqueous solution. PMID: 22154267
8. Interaction between 2',4-dihydroxychalcone and the N, f, e conformers of albumin was exothermic and spontaneous. PMID: 22450828
9. serum albumin possesses chaperone-like properties and that this activity is maintained under a number of physiologically relevant conditions. PMID: 22549788
10. The dynamics of bovine serum albumin (BSA) and human fibrinogen (Fg) at low concentrations were observed at the solid-aqueous interface as a function of temperature. PMID: 22713578
11. A crystallographic structural study allows identification of serum albumin fragments responsible for immunogenicity and the postulation of a mechanism for antigen-antibody recognition in cattle. PMID: 22993082
12. Bovine Serum Albumine aqueous solutions in the presence of NaCl are investigated for different protein concentrations and low to intermediate ionic strengths. Protein interactions are modeled via a charge-screened colloidal model. PMID: 23534667
13. Data (including data from biophysical studies using Langmuir lipid monolayer technique) suggest that human/bovine ALB exhibits minimal electrostatic repulsion and inserts effectively into phospholipid monolayers. [REVIEW] PMID: 24267981
14. molecular modeling approaches were employed to determine the interaction between lysionotin and bovine serum albumin (BSA) at physiological pH PMID: 24398555
15. Data suggest that native BSA samples can be dehydrated to approximately 450 waters per protein molecule via microglassification and then reverted to native-like conformation upon rehydration with only minor irreversible aggregation. PMID: 24415208
16. The ITC results indicated that the interaction between the protein (BSA and BHb) and QDs-612 was spontaneous and the predominant force was hydrophobic interaction PMID: 25143002
17. data indicate that conjugation of carboxyl groups with monosaccharide generates functional BSA with membrane-perturbing activities on the lipid-water interface. PMID: 25449061
18. Data show that the maximum adsorption occurred at the isoelectric point (pH 4.7) of bovine serum albumin (BSA). PMID: 26673525
19. Degradation of BSA by serine proteases was monitored with Fourier transform infrared (FT-IR) and ultraviolet circular dichroism (UV-CD). alpha-Helical structure of BSA was converted into unordered structure upon digestion. PMID: 26926394
20. Molecular dynamics (MD) simulation results demonstrate that the "hard protein" lysozyme retains much of its secondary structure during adsorption, whereas BSA loses it almost completely. BSA has a considerably larger adsorption energy compared to that of lysozyme, which does not scale with chain length. Desorption simulations are carried out using classical steered MD. PMID: 27421144
21. that thiamine hydrochloride (TA) is located in site I of bovine serum albumin (BSA). PMID: 27550086
22. identified a total of 125 carbonylated residues in bovine serum albumin after extensive in vitro metal ion-catalysed oxidation PMID: 28062376
23. The molecular dynamics results show how the negatively charged BSA at pH7 adsorbs to the negatively charged silica surface, and reveal a unique orientation with preserved secondary and tertiary structure. The experiments then show that the protein forms complete monolayers at approximately pH6, just above the protein's isoelectric point (pH5.1). PMID: 28350173
24. The interaction of DRV with bovine serum albumin (BSA), a major carrier protein, has been studied under simulated physiological conditions (pH7.4) by multi-spectroscopic techniques in combination with molecular modeling. PMID: 28753530
25. hese obtained results provide an in-depth understanding of the interaction of the acid azo dye AO10 with serum albumins. PMID: 29126006

KEGG: bta:280717

STRING: 9913.ENSBTAP00000022763

UniGene: Bt.106669