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).

The Solubility of Insect Juvenile Hormone in Aqueous Solutions and Its Adsorption by Glassware and Plastics

1977 ◽  
Vol 32 (3-4) ◽  
pp. 158-160 ◽  
Author(s):  
Ch. Giese ◽  
K. D. Spindler ◽  
H. Emmerich
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Juvenile Hormone ◽  
Immunoglobulin G ◽  
Bovine Serum ◽  
Plastic Materials ◽  
Buffer Composition ◽  
Ph Buffer

Abstract The C18 juvenile hormone of insects can be dissolved in aqueous solutions up to a concentration of 2.5 - 3.0 × 10-5 M; changes in pH, buffer composition and ionic strength hardly affect this solu­bility. The hormone is salted out gradually by increasing ammonium sulphate concentrations. The juvenile hormone is bound to proteins such as bovine serum albumin or goat immunoglobulin G and can be kept in solution by these proteins up to 10-3 M. The hormone is strongly absorbed by many commonly used plastic materials but only to a lesser extent by glass and teflon.

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