scholarly journals Bovine serum albumin oligomers in the E- and B-forms at low protein concentration and ionic strength

2013 ◽  
Vol 53 ◽  
pp. 42-53 ◽  
Author(s):  
Jeremiah J. Babcock ◽  
Lorenzo Brancaleon
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Low Protein

scholarly journals The effect of ionic strength on the rheology of pH-induced bovine serum albumin/κ-carrageenan coacervates

LWT ◽  
2014 ◽  
Vol 59 (1) ◽  
pp. 356-360 ◽  
Author(s):  
Changhoon Chai ◽  
Jooyoung Lee ◽  
Qingrong Huang
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

Studies on Characteristics and Adsorption of BSA on Hydrogel Biomaterials

2007 ◽  
Vol 330-332 ◽  
pp. 901-904
Author(s):  
G.X. Tan ◽  
Ying De Cui ◽  
Ying Jun Wang
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Chemical Stability ◽  
Contact Lens ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Radical Copolymerization ◽  
Vinyl Pyrrolidone ◽  
Equilibrium Water Content ◽  
Influence Of Ph

Hydrogel biomaterials were synthesized by radical copolymerization of N-vinyl pyrrolidone (NVP) and 2-hydroxyethylmathacrylate (HEMA), with azobisisobutyronitrile (AIBN) as an initiator, reacting at 60~70°C for 24 hours, which were designed as contact lens due to the good chemical stability and high biocompatibility. The absorbency of bovine serum albumin (BSA) was measured by the ultraviolet spectrophotometer. The influence of pH, initial protein concentration and ionic strength were investigated in detail. The results showed that the absorption of protein on hydrogel biomaterials increased with the immersing time increasing, and was stable during 4 days. The absorption of protein on hydrogel increased with the equilibrium water content increasing. The protein absorption on hydrogels reduced the permeability of the oxygen of the biomaterials.

The precipitation of proteins by carboxymethyl cellulose

1975 ◽  
Vol 42 (2) ◽  
pp. 267-275 ◽  
Author(s):  
J. G. Zadow ◽  
R. D. Hill
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Carboxymethyl Cellulose ◽  
Degree Of Substitution ◽  
Maximum Precipitation ◽  
Ph Range ◽  
High Degree ◽  
Β Lactoglobulin

SummaryCarboxymethyl cellulose (CMC) formed insoluble complexes with β-lactoglobulin, bovine serum albumin and Na caseinate. Maximum precipitation of the β-lactoglobulin-CMC complex occurred at pH 3·2, whereas maximum precipitation of the bovine serum albumin-CMC complex and the Na caseinate-CMC complex occurred at pH 2·8. The ratio of CMC to protein for maximum precipitation depended on the protein, being greatest for Na caseinate and least for bovine serum albumin. The percentage of protein precipitated by CMC decreased with increasing ionic strength of the solution, the rate of decrease being least for bovine serum albumin. At a given ionic strength, more protein was precipitated by CMC of high degree of substitution than by CMC of low degree of substitution. The change in pH (ΔpH) occurring on mixing CMC and unbuffered protein solutions, each initially at the same pH, was measured. ΔpH was negative for β-lactoglobulin-CMC mixtures over the pH range 7–2 (minimum at pH 5·5). For bovine serum albumin-CMC and Na caseinate-CMC mixtures, ΔpH was positive between pH 7 and 3·2 (maximum at pH 4·5), zero at pH 3·2 and negative between pH 3·2 and 2·0 (minimum at pH 2·8).

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.

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