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Protein Isolation by Solution‐Controlled Gel Sorption
Author(s) -
Gehrke Stevin H.,
Robeson Julie,
Johnson James Fred,
Vaid Nitin
Publication year - 1991
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00010a010
Subject(s) - sorption , chromatography , chemistry , peg ratio , ethylene glycol , polymer , ovalbumin , bovine serum albumin , aqueous solution , phase (matter) , extraction (chemistry) , protein purification , dextran , polymer chemistry , organic chemistry , adsorption , immune system , finance , immunology , economics , biology
Abstract Illustrated are the principles for isolating proteins from solution by sorption into a polymer gel phase, driven by the addition of a water‐soluble polymer to the protein solution. The separation is shown to be analogous to conventional two‐phase aqueous extraction. However, the use of a gel phase rather than a solution for absorbing the protein makes separation of the protein from the polymer and the recycling of the gel phase much simpler. The model system used was linear poly(ethylene glycol) (PEG) and dextran gel. Increasing the molecular weight and concentration of the PEG favored sorption by the gel of ovalbumin, bovine serum albumin, cytochrome c , and hemoglobin. The proteins could be quantitatively recovered by immersing the gel in PEG‐free solution.