Effects of pH, salt type, and ionic strength on the second virial coefficients of aqueous bovine serum albumin solutions

2009 ◽  
Vol 26 (1) ◽  
pp. 193-198 ◽  
Author(s):  
YoonKook Park ◽  
Ginkyu Choi
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Virial Coefficients ◽  
Second Virial Coefficients ◽  
Effects Of Ph

Gelation of bovine serum albumin and β-lactoglobulin; effects of pH, salts and thiol reagents

1991 ◽  
Vol 40 (1) ◽  
pp. 55-69 ◽  
Author(s):  
Naotoshi Matsudomi ◽  
Douglas Rector ◽  
J.E. Kinsella
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Effects Of Ph ◽  
Β Lactoglobulin

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

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).

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