Conformational stability of a model protein (bovine serum albumin) during primary emulsification process of PLGA microspheres synthesis

2003 ◽  
Vol 260 (1) ◽  
pp. 149-156 ◽  
Author(s):  
F Kang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Conformational Stability ◽  
Plga Microspheres ◽  
Model Protein ◽  
Protein Bovine Serum Albumin ◽  
Emulsification Process

Alteration of water absorption in the THz region traces the onset of fibrillation in proteins

2021 ◽  
Author(s):  
Partha Pyne ◽  
Nirnay Samanta ◽  
Himanshu Gohil ◽  
S. S. Prabhu ◽  
Rajib Kumar Mitra
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Water Absorption ◽  
Bovine Serum ◽  
Terahertz Spectroscopy ◽  
Model Protein ◽  
Protein Bovine Serum Albumin

Using terahertz spectroscopy, we established the alteration of the collective hydration of water during the fibrillation process (native → intermediate → fibril) of a model protein bovine serum albumin.

scholarly journals Efficacy of alcohol/sugar aqueous biphasic system on partition of bovine serum albumin

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Yin Hui Chow ◽  
Alagan Sahlini ◽  
Hui-Suan Ng ◽  
John Chi-Wei Lan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Protein Extraction ◽  
Ftir Analysis ◽  
Model Protein ◽  
Aqueous Biphasic ◽  
The Fourier Transform ◽  
Protein Bovine Serum Albumin

AbstractThe efficacy of alcohol/sugar aqueous biphasic (ABS) system on protein extraction was investigated. A model protein, bovine serum albumin (BSA), was adopted to evaluate the effects of types and concentration of phase-forming components, protein concentration, and system pH on the protein partition efficiency. The 1-propanol/maltose ABS exhibited an overall better partition efficiency of BSA to the alcohol-rich top phase. A maximum partition coefficient (K) of 20.01 ± 0.05 and recovery yield (Y) of 95.42% ± 0.01% of BSA were achieved with 35% (w/w) 1-propanol/22% (w/w) maltose ABS at pH 5.0 for 10% (w/w) BSA load. The K and Y of BSA in 1-propanol/maltose ABS was slightly improved with the addition of 3% (w/w) of ionic liquid, 1-butyl-3-methylimidazolium bromide ([Bmim]Br) as the adjuvant that could provide protein stabilizing effect. The Fourier Transform Infrared Spectrum (FTIR) analysis revealed that the protein structure remained unaltered upon the separation process.

scholarly journals Isotachophoresis-based sample preparation of cellulases in sugarcane juice using bovine serum albumin as a model protein

2010 ◽  
Vol 1217 (51) ◽  
pp. 8026-8031 ◽  
Author(s):  
Ruchi Gupta ◽  
Sara J. Baldock ◽  
Peter R. Fielden ◽  
Jeff E. Prest ◽  
Bruce D. Grieve
Keyword(s):  
Bovine Serum Albumin ◽  
Sample Preparation ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sugarcane Juice ◽  
Model Protein

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.

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