Thermo-reversibility, ergodicity and surface charge–temperature dependent phase diagram of anionic, cationic and neutral co-gels of gelatin–BSA complexes

RSC Advances ◽  
2016 ◽  
Vol 6 (46) ◽  
pp. 40123-40136 ◽  
Author(s):  
Jyotsana Pathak ◽  
Kamla Rawat ◽  
H. B. Bohidar
Keyword(s):  
Phase Diagram ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Mixing Ratio ◽  
Temperature Dependent ◽  
Gelation Behavior ◽  
Ph Range ◽  
Protein Bovine Serum Albumin ◽  
Charge Temperature

We have investigated the gelation behavior of polyampholyte gelatin B (GB) in the presence of colloidal plasma protein bovine serum albumin (BSA) as a function of mixing ratio (r = GB : BSA = 1.5–4), entire pH range, and temperature (20–45 °​C).

Influence of Terahertz Radiation of Various Ranges on Molecule Conformation of Bovine Serum Albumin

2010 ◽  
Vol 5 (4) ◽  
pp. 182-185
Author(s):  
Angelina V. Kapralova ◽  
Aleksandr S. Pogodin
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Radiation Power ◽  
Uv Spectrophotometry ◽  
Absorption Bands ◽  
Conformation Changes ◽  
Protein Molecules ◽  
Molecule Conformation ◽  
Protein Bovine Serum Albumin

We investigated the influence of THz laser radiation of frequencies of 1.15 THz and 3.68 THz and radiation power of about 10 Mw on protein (bovine serum albumin). Using UV spectrophotometry, we revealed increase in the optical density of irradiated samples of bovine serum albumin at the characteristic absorption bands, which is evidence of conformation changes in protein molecules

scholarly journals The Glass Transition Behavior of the Globular Protein Bovine Serum Albumin

2003 ◽  
Vol 85 (6) ◽  
pp. 3943-3950 ◽  
Author(s):  
Geoffrey J. Brownsey ◽  
Timothy R. Noel ◽  
Roger Parker ◽  
Stephen G. Ring
Keyword(s):  
Glass Transition ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Globular Protein ◽  
Transition Behavior ◽  
Protein Bovine Serum Albumin

scholarly journals Anomalous protein kinetics on low-fouling surfaces

2020 ◽  
Vol 22 (9) ◽  
pp. 5264-5271
Author(s):  
Mohammadhasan Hedayati ◽  
Matt J. Kipper ◽  
Diego Krapf
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Single Molecule ◽  
Bovine Serum ◽  
Time Distribution ◽  
Dwell Time ◽  
Protein Kinetics ◽  
Single Molecule Tracking ◽  
Heavy Tailed ◽  
Protein Bovine Serum Albumin

Single-molecule tracking reveals the protein bovine serum albumin exhibits anomalous kinetics with a heavy-tailed dwell time distribution on PEG surfaces. This effect is shown to be caused by the ability of the protein to oligomerize in solution.

scholarly journals Binding Aspects of 2-(4-Hydroxyphenylazo)benzoic Acid to Bovine Serum Albumin in the Limited Mixing Ratio

1988 ◽  
Vol 61 (8) ◽  
pp. 2727-2730
Author(s):  
Kunio Takeda ◽  
Katsushi Sasa ◽  
Kazuaki Hachiya ◽  
Mamoru Murata ◽  
Koichiro Aoki
Keyword(s):  
Bovine Serum Albumin ◽  
Benzoic Acid ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Mixing Ratio

Pressure Jump Studies of Proteins. I. Isomerization of Bovine Serum Albumin at Neutral pH

1971 ◽  
Vol 49 (12) ◽  
pp. 1267-1275 ◽  
Author(s):  
D. E. Goldsack ◽  
P. M. Waern
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Change ◽  
Bovine Serum ◽  
Ph Dependence ◽  
Kinetic Studies ◽  
Relaxation Effect ◽  
Pressure Jump ◽  
Relaxation Effects ◽  
Ph Range

Pressure jump kinetic studies of the conformational change occurring in bovine serum albumin in neutral solutions have been carried out over the pH range 6.5–9.5. Two distinct relaxation effects are observed at each pH. The faster relaxation is attributed to binding of the dye to the protein, and the slower relaxation is related to the conformational change occurring in the protein. This slower relaxation effect is pH dependent with a maximum value near pH 8. Detailed analysis of these data leads to a mechanism for the conformational change which indicates that the one form of the protein has an ionizable group with a pK of 8.7 which changes to a pK of 6.7 when the protein undergoes the conformational change. A simple iterative procedure is given for analyzing the pH dependence of a relaxation time constant for a cyclic mechanism involving only one ionizing group controlling the conformational change.

scholarly journals Direct evidence for the involvement of domain III in the N-F transition of bovine serum albumin

1986 ◽  
Vol 236 (1) ◽  
pp. 307-310 ◽  
Author(s):  
M Y Khan
Keyword(s):  
Bovine Serum Albumin ◽  
Acid Solution ◽  
Serum Albumin ◽  
Protein Sequence ◽  
Bovine Serum ◽  
Direct Evidence ◽  
Structural Transformations ◽  
The Other ◽  
Ph Range ◽  
Domain Iii

The domain III of bovine serum albumin containing residues 377-582 of the protein sequence was isolated and its behaviour in acid solution was studied. The fragment was found to undergo structural transformations over the pH range 3.5-4.5 known to cause N-F transition in serum albumin. On the other hand, an albumin fragment that was devoid of domain III was unable to exhibit such a transition. These results were consistent with a mechanism where N-F transition involves the separation of domain III from the rest of the albumin starts at about pH 4.3 and is completed at pH 3.5.

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